Cytochrome C -Adis - Revision history

Michal Harel at 09:26, 9 January 2020

Michal Harel — Thu, 09 Jan 2020 09:26:46 GMT

←Older revision		Revision as of 09:26, 9 January 2020
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	==Cytochrome ''C''==		==Cytochrome ''C''==
	<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme and sulfate complex (PDB code [[3cp5]])' scene=''>		<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme and sulfate complex (PDB code [[3cp5]])' scene=''>
-	~~Cytochrome~~ ''C'' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is normally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome ''C'' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome ''C'' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome ''C'' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome ''C'' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome ''C'', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome ''C'' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome ''C'' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome ''C'' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.	+	'''Cytochrome C''' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is normally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome ''C'' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome ''C'' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome ''C'' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome ''C'' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome ''C'', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome ''C'' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome ''C'' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome ''C'' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.

	== Structure ==		== Structure ==

Michal Harel at 09:23, 9 January 2020

Michal Harel — Thu, 09 Jan 2020 09:23:20 GMT

←Older revision		Revision as of 09:23, 9 January 2020
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	==Cytochrome ''C''==		==Cytochrome ''C''==
-	<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>	+	<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme and sulfate complex (PDB code [[3cp5]])' scene=''>
	Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is normally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome ''C'' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome ''C'' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome ''C'' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome ''C'' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome ''C'', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome ''C'' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome ''C'' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome ''C'' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.		Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is normally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome ''C'' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome ''C'' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome ''C'' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome ''C'' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome ''C'', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome ''C'' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome ''C'' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome ''C'' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.

Adis Hasic at 00:32, 4 May 2019

Adis Hasic — Sat, 04 May 2019 00:32:04 GMT

←Older revision		Revision as of 00:32, 4 May 2019
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	functions in eukaryotes the electron transport chain. Cytochrome ''C'' is an electron		functions in eukaryotes the electron transport chain. Cytochrome ''C'' is an electron
	transfer protein during the bc1 complex of the electron transport chain. (See below for more		transfer protein during the bc1 complex of the electron transport chain. (See below for more
-	detailed information) Involving identical structure to the ~~Cytochrome ''C'' protein in~~ <scene name='81/814739/Bc1_complex_cytc/1'>mitochondria</scene>,	+	detailed information) Involving identical structure to the <scene name='81/814739/Bc1_complex_cytc/1'>Cytochrome ''C'' protein in mitochondria</scene>,
	one conformation of Cytochrome ''C'' is also a member of the electron transport chain in		one conformation of Cytochrome ''C'' is also a member of the electron transport chain in
	photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.)		photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.)

Adis Hasic at 00:30, 4 May 2019

Adis Hasic — Sat, 04 May 2019 00:30:44 GMT

Adis Hasic at 00:16, 4 May 2019

Adis Hasic — Sat, 04 May 2019 00:16:37 GMT

←Older revision		Revision as of 00:16, 4 May 2019
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-	==Cytochrome ~~"C"~~==	+	==Cytochrome ''c''==
	<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>		<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>
	Cytochrome "C" is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome 'C' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.		Cytochrome "C" is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome 'C' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.

Adis Hasic at 00:15, 4 May 2019

Adis Hasic — Sat, 04 May 2019 00:15:34 GMT

←Older revision		Revision as of 00:15, 4 May 2019
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-	==Cytochrome 'C'==	+	==Cytochrome "C"==
	<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>		<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>
-	Cytochrome 'C' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different ~~conformations~~ of Cytochrome 'C' cause it to have different functions overall. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, ~~is one~~ of ~~the most experimented on proteins out there~~. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established ~~itself~~ in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.	+	Cytochrome "C" is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome 'C' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.

	== Structure ==		== Structure ==

Adis Hasic at 00:05, 4 May 2019

Adis Hasic — Sat, 04 May 2019 00:05:54 GMT

Adis Hasic at 21:29, 3 May 2019

Adis Hasic — Fri, 03 May 2019 21:29:06 GMT

Adis Hasic at 20:21, 3 May 2019

Adis Hasic — Fri, 03 May 2019 20:21:22 GMT

←Older revision		Revision as of 20:21, 3 May 2019
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	cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central		cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central
	iron atom. They can form different compounds by having different attachments around the 4		iron atom. They can form different compounds by having different attachments around the 4
-	pyrrole rings. Two conformations of cytochrome C exist naturally but both having the same general <scene name='Sandbox_Reserved_335/Motif/1'>structure</scene>. In the monoheme	+	pyrrole rings. Two conformations of cytochrome C exist naturally but both having the same general motif or <scene name='Sandbox_Reserved_335/Motif/1'>structure</scene>. In the monoheme
	form, the other axial position is usually left empty however, it can be occupied by other		form, the other axial position is usually left empty however, it can be occupied by other
	molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and		molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and

Adis Hasic at 20:20, 3 May 2019

Adis Hasic — Fri, 03 May 2019 20:20:41 GMT

←Older revision		Revision as of 20:20, 3 May 2019
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	cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central		cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central
	iron atom. They can form different compounds by having different attachments around the 4		iron atom. They can form different compounds by having different attachments around the 4
-	pyrrole rings. Two conformations of cytochrome C exist naturally. In the monoheme	+	pyrrole rings. Two conformations of cytochrome C exist naturally but both having the same general <scene name='Sandbox_Reserved_335/Motif/1'>structure</scene>. In the monoheme
	form, the other axial position is usually left empty however, it can be occupied by other		form, the other axial position is usually left empty however, it can be occupied by other
	molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and		molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and

←Older revision		Revision as of 00:30, 4 May 2019
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-	==Cytochrome ''c''==	+	==Cytochrome ''C''==
	<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>		<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>
-	Cytochrome "C" is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is ~~generally~~ located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome 'C' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.	+	Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is normally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome ''C'' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome ''C'' into the cytosol in order to initiate apoptosis. Different attachments to the central heme group of Cytochrome ''C'' cause it to have different functions overall. The protein structure and function differ, but it is still considered to be a Cytochrome C protein. The composition of Cytochrome ''C'' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome ''C'', since it is so small, it has been the subject of many experiments. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes.(New Journal of Science). It is also an ancient protein that was established in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome ''C'' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome ''C'' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome ''C'' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.

	== Structure ==		== Structure ==
-	Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a	+	Cytochrome ''C'' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a
	heme prosthetic group. This <scene name='Sandbox_Reserved_335/Axial/6'>heme prosthetic</scene> group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central		heme prosthetic group. This <scene name='Sandbox_Reserved_335/Axial/6'>heme prosthetic</scene> group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central
	iron atom. They can form different compounds by having different attachments around the 4		iron atom. They can form different compounds by having different attachments around the 4
-	pyrrole rings. Two unique structures of Cytochrome 'C' exist naturally but both having the same general motif or <scene name='Sandbox_Reserved_335/Motif/1'>basic structure</scene>. In the monoheme	+	pyrrole rings. Two unique structures of Cytochrome ''C'' exist naturally but both having the same general motif or <scene name='Sandbox_Reserved_335/Motif/1'>basic structure</scene>. In the monoheme
	form, the other axial position is usually left empty however, it can be occupied by other		form, the other axial position is usually left empty however, it can be occupied by other
	molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and		molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and
	allows for easier attachment. The other forms contain anywhere from one to four methionine		allows for easier attachment. The other forms contain anywhere from one to four methionine
	groups on the occupied side of the heme group. When drawn out, the structure of		groups on the occupied side of the heme group. When drawn out, the structure of
-	Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior	+	Cytochrome ''C'' looks vertically and horizontally symmetrical due to the central heme group prior
	to adding side chains. The side chains which determine overall function are branched off of the		to adding side chains. The side chains which determine overall function are branched off of the
	central heme group and vary depending on the proteins location in the cell. They can have one		central heme group and vary depending on the proteins location in the cell. They can have one
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	== Function ==		== Function ==
-	Cytochrome 'C' function is dependent on the conformation of the structure it is portraying	+	Cytochrome ''C'' function is dependent on the conformation of the structure it is portraying
-	at the time which is primarily determined by the location of the Cytochrome 'C' protein within the	+	at the time which is primarily determined by the location of the Cytochrome ''C'' protein within the
-	cell. Monoheme Cytochrome 'C', which is primarily found in the mitochondria of the cell,	+	cell. Monoheme Cytochrome ''C'', which is primarily found in the mitochondria of the cell,
-	functions in eukaryotes the electron transport chain. Cytochrome 'C' is an electron	+	functions in eukaryotes the electron transport chain. Cytochrome ''C'' is an electron
	transfer protein during the bc1 complex of the electron transport chain. (See below for more		transfer protein during the bc1 complex of the electron transport chain. (See below for more
-	detailed information) Involving identical structure to the Cytochrome 'C' protein in <scene name='81/814739/Bc1_complex_cytc/1'>mitochondria</scene>,	+	detailed information) Involving identical structure to the Cytochrome ''C'' protein in <scene name='81/814739/Bc1_complex_cytc/1'>mitochondria</scene>,
-	one conformation of Cytochrome 'C' is also a member of the electron transport chain in	+	one conformation of Cytochrome ''C'' is also a member of the electron transport chain in
	photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.)		photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.)
-	Cytochrome 'C' is also a main signaling factor for	+	Cytochrome ''C'' is also a main signaling factor for
-	apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the	+	apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome ''C'' plays a key role in the
-	initiation of cell death. Without Cytochrome 'C', the cell could not release the protein into the	+	initiation of cell death. Without Cytochrome ''C'', the cell could not release the protein into the
	cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed		cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed
	information on this function)		information on this function)
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	to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer		to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer
	lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell		lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell
-	Death) Cytochrome 'C' takes play in the intrinsic pathway. This is when a stimulus causes	+	Death) Cytochrome ''C'' takes play in the intrinsic pathway. This is when a stimulus causes
-	Cytochrome 'C' to be released into the Cytosol. Once cytochrome 'C' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing	+	Cytochrome ''C'' to be released into the Cytosol. Once cytochrome ''C'' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing
	apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting		apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting
	old, it has degradation of its membranes. This degradation also leads to the release of		old, it has degradation of its membranes. This degradation also leads to the release of
-	Cytochrome 'C' which would signal that the cell is old and ready to be killed off. Without	+	Cytochrome ''C'' which would signal that the cell is old and ready to be killed off. Without
-	Cytochrome 'C', intrinsic apoptosis would not be possible because the apoptotic factors would	+	Cytochrome ''C'', intrinsic apoptosis would not be possible because the apoptotic factors would
-	never be activated. Same as if there are mutations in Cytochrome 'C' causing it to be unable to	+	never be activated. Same as if there are mutations in Cytochrome ''C'' causing it to be unable to
	permeate through the membrane, or if there is a mutation that increases the permeability of it		permeate through the membrane, or if there is a mutation that increases the permeability of it
	through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C		through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C
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	== Purpose in ETC and Photosynthesis ==		== Purpose in ETC and Photosynthesis ==
-	Cytochrome 'C' also plays a key role in the Electron Transport Chain in mitochondria. It is one of	+	Cytochrome ''C'' also plays a key role in the Electron Transport Chain in mitochondria. It is one of
	the many electron carriers in the electron transport chain but quite a vital one. The heme group		the many electron carriers in the electron transport chain but quite a vital one. The heme group
-	portion of Cytochrome 'C' accepts the electrons from the bc1 complex and then carries the	+	portion of Cytochrome ''C'' accepts the electrons from the bc1 complex and then carries the
-	electrons to complex IV. Once at complex IV, the Cytochrome 'C' release their electron that they	+	electrons to complex IV. Once at complex IV, the Cytochrome ''C'' release their electron that they
-	are carrying and it is given to the Cytochrome 'C' Oxidase enzyme. This enzyme accumulates 4	+	are carrying and it is given to the Cytochrome ''C'' Oxidase enzyme. This enzyme accumulates 4
	electrons and transfers them to one dioxygen		electrons and transfers them to one dioxygen
	molecule in order to make two molecules of water. It is also found within the thylakoid		molecule in order to make two molecules of water. It is also found within the thylakoid
	membrane in the chloroplast of plants and green algae. In photosynthesis,		membrane in the chloroplast of plants and green algae. In photosynthesis,
-	Cytochrome 'C' is one of the steps that transfers electrons from photosystem II to photosystem I.	+	Cytochrome ''C'' is one of the steps that transfers electrons from photosystem II to photosystem I.
	Later in the cycle, the electrochemical gradient will		Later in the cycle, the electrochemical gradient will
	then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)		then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)
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	== Medical/Research Purposes ==		== Medical/Research Purposes ==
	A proposal by many research scientists has been to regulate mitochondrial energy		A proposal by many research scientists has been to regulate mitochondrial energy
-	production and ROS production through the phosphorylation of cytochrome 'C'. It has been	+	production and ROS production through the phosphorylation of cytochrome ''C''. It has been
-	observed that Tyr48Glu phosphomimetic mutant Cytochrome 'C' reacts with CcO, but it is	+	observed that Tyr48Glu phosphomimetic mutant Cytochrome ''C'' reacts with CcO, but it is
	partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome		partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome
	c) They are proposing that “this effect plays an essential role in the prevention of ROS under		c) They are proposing that “this effect plays an essential role in the prevention of ROS under
-	healthy conditions.” There is evidence when cellular stress is happening, Cytochrome 'C' then	+	healthy conditions.” There is evidence when cellular stress is happening, Cytochrome ''C'' then
	becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets		becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets
-	up Cytochrome 'C' to initiate apoptosis. They report that the cellular stress causes mitochondrial	+	up Cytochrome ''C'' to initiate apoptosis. They report that the cellular stress causes mitochondrial
	membrane potential differences and it needs to be taken into account to be able to determine the		membrane potential differences and it needs to be taken into account to be able to determine the
	risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of		risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of
-	Cytochrome 'C', but acknowledges the fact that other factors may also be affected through their	+	Cytochrome ''C'', but acknowledges the fact that other factors may also be affected through their
	actions. Others have began to focus their research on major diseases such as Huntington’s		actions. Others have began to focus their research on major diseases such as Huntington’s
	disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the		disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the
	closest that anyone has come to a universal cure for cancers has been with the use of the		closest that anyone has come to a universal cure for cancers has been with the use of the
-	apoptotic function of Cytochrome 'C'. They went on to explain that tricking the body into	+	apoptotic function of Cytochrome ''C''. They went on to explain that tricking the body into
	believing these cancerous cells are ready to die, they could negate the effects of the ineffective		believing these cancerous cells are ready to die, they could negate the effects of the ineffective
	p53 gene.		p53 gene.

←Older revision		Revision as of 00:05, 4 May 2019
Line 5:		Line 5:
	== Structure ==		== Structure ==
	Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a		Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a
-	heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to	+	heme prosthetic group. This <scene name='Sandbox_Reserved_335/Axial/6'>heme prosthetic</scene> group is covalently bonded using thioether bonds to Histidine and Methionine residues. This heme prosthetic is four cyclic structures forming a macrocycle which coordinates functionality about a central
-	~~cysteine~~ residues. This heme prosthetic is four cyclic structures forming a ~~circle around~~ a central	+
	iron atom. They can form different compounds by having different attachments around the 4		iron atom. They can form different compounds by having different attachments around the 4
-	pyrrole rings. Two ~~conformations~~ of Cytochrome 'C' exist naturally but both having the same general motif or <scene name='Sandbox_Reserved_335/Motif/1'>structure</scene>. In the monoheme	+	pyrrole rings. Two unique structures of Cytochrome 'C' exist naturally but both having the same general motif or <scene name='Sandbox_Reserved_335/Motif/1'>basic structure</scene>. In the monoheme
	form, the other axial position is usually left empty however, it can be occupied by other		form, the other axial position is usually left empty however, it can be occupied by other
	molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and		molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and
-	allows for easier attachment. The other forms contain anywhere from one to ~~seven~~ methionine	+	allows for easier attachment. The other forms contain anywhere from one to four methionine
-	groups on ~~what we perceive~~ the ~~left~~ side of the heme group. When drawn out, the structure of	+	groups on the occupied side of the heme group. When drawn out, the structure of
	Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior		Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior
	to adding side chains. The side chains which determine overall function are branched off of the		to adding side chains. The side chains which determine overall function are branched off of the
Line 28:		Line 27:
	detailed information) Involving identical structure to the Cytochrome 'C' protein in <scene name='81/814739/Bc1_complex_cytc/1'>mitochondria</scene>,		detailed information) Involving identical structure to the Cytochrome 'C' protein in <scene name='81/814739/Bc1_complex_cytc/1'>mitochondria</scene>,
	one conformation of Cytochrome 'C' is also a member of the electron transport chain in		one conformation of Cytochrome 'C' is also a member of the electron transport chain in
-	photosynthesis in plants ~~and cyanobacteria~~. (PDB101: Molecule of the Month: Cytochrome c.)	+	photosynthesis in plants. (PDB101: Molecule of the Month: Cytochrome c.)
	Cytochrome 'C' is also a main signaling factor for		Cytochrome 'C' is also a main signaling factor for
	apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the		apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the

←Older revision		Revision as of 21:29, 3 May 2019
Line 1:		Line 1:
-	==Cytochrome C==	+	==Cytochrome 'C'==
	<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>		<StructureSection load='3CP5' size='340' side='right' caption='Cytochrome C with a heme complex' scene=''>
-	Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of ~~cytochrome~~ C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.	+	Cytochrome 'C' is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome 'C' is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of Cytochrome 'C' into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome 'C' cause it to have different functions overall. The composition of Cytochrome 'C' is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome 'C', since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome 'C' was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome 'C' release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome 'C' in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.

	== Structure ==		== Structure ==
-	Cytochrome C is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a	+	Cytochrome 'C' is a [http://en.wikipedia.org/wiki/Heme heme] protein (or a part of the heme family) which means that it has a
	heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to		heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to
	cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central		cysteine residues. This heme prosthetic is four cyclic structures forming a circle around a central
	iron atom. They can form different compounds by having different attachments around the 4		iron atom. They can form different compounds by having different attachments around the 4
-	pyrrole rings. Two conformations of ~~cytochrome~~ C exist naturally but both having the same general motif or <scene name='Sandbox_Reserved_335/Motif/1'>structure</scene>. In the monoheme	+	pyrrole rings. Two conformations of Cytochrome 'C' exist naturally but both having the same general motif or <scene name='Sandbox_Reserved_335/Motif/1'>structure</scene>. In the monoheme
	form, the other axial position is usually left empty however, it can be occupied by other		form, the other axial position is usually left empty however, it can be occupied by other
	molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and		molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and
	allows for easier attachment. The other forms contain anywhere from one to seven methionine		allows for easier attachment. The other forms contain anywhere from one to seven methionine
	groups on what we perceive the left side of the heme group. When drawn out, the structure of		groups on what we perceive the left side of the heme group. When drawn out, the structure of
-	Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior	+	Cytochrome 'C' looks vertically and horizontally symmetrical due to the central heme group prior
	to adding side chains. The side chains which determine overall function are branched off of the		to adding side chains. The side chains which determine overall function are branched off of the
	central heme group and vary depending on the proteins location in the cell. They can have one		central heme group and vary depending on the proteins location in the cell. They can have one
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	== Function ==		== Function ==
-	Cytochrome C function is dependent on the conformation of the structure it is portraying	+	Cytochrome 'C' function is dependent on the conformation of the structure it is portraying
-	at the time which is primarily determined by the location of the ~~cytochrome c~~ protein within the	+	at the time which is primarily determined by the location of the Cytochrome 'C' protein within the
-	cell. Monoheme ~~cytochrome~~ C, which is primarily found in the mitochondria of the cell,	+	cell. Monoheme Cytochrome 'C', which is primarily found in the mitochondria of the cell,
-	functions in eukaryotes the electron transport chain. Cytochrome C is an electron	+	functions in eukaryotes the electron transport chain. Cytochrome 'C' is an electron
	transfer protein during the bc1 complex of the electron transport chain. (See below for more		transfer protein during the bc1 complex of the electron transport chain. (See below for more
-	detailed information) Involving identical structure to the ~~cytochrome~~ C protein in <scene name='81/814739/Bc1_complex_cytc/1'>mitochondria</scene>,	+	detailed information) Involving identical structure to the Cytochrome 'C' protein in <scene name='81/814739/Bc1_complex_cytc/1'>mitochondria</scene>,
-	one conformation of ~~cytochrome~~ C is also a member of the electron transport chain in	+	one conformation of Cytochrome 'C' is also a member of the electron transport chain in
	photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.)		photosynthesis in plants and cyanobacteria. (PDB101: Molecule of the Month: Cytochrome c.)
-	~~You can also find it in a Heme C form which is a membrane bound protein that converts O2 into~~	+	Cytochrome 'C' is also a main signaling factor for
-	~~two water molecules using the electrons.~~ Cytochrome C is also a main signaling factor for	+	apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome 'C' plays a key role in the
-	apoptosis of cells. In the intrinsic pathway of apoptosis, Cytochrome C plays a key role in the	+	initiation of cell death. Without Cytochrome 'C', the cell could not release the protein into the
-	initiation of cell death. Without Cytochrome C, the cell could not release the protein into the	+
	cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed		cytosol which at high volumes leads to intrinsic apoptosis. (see below for more detailed
	information on this function)		information on this function)
Line 43:		Line 42:
	to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer		to perform apoptosis. During the extrinsic pathway, an immune response is initiated by killer
	lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell		lymphocytes which cause an apoptotic cascade. (Apoptosis: a Review of Programmed Cell
-	Death) Cytochrome C takes play in the intrinsic pathway. This is when a stimulus causes	+	Death) Cytochrome 'C' takes play in the intrinsic pathway. This is when a stimulus causes
-	Cytochrome C to be released into the Cytosol. Once cytochrome C is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing	+	Cytochrome 'C' to be released into the Cytosol. Once cytochrome 'C' is in the cytosol, it is recognized and bound to apoptotic factors which are then activated forming the apoptosome complex. Then caspases join in and are activated which result in a caspase cascade forcing
	apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting		apoptosis. (Cytochrome c: Functions beyond Respiration.) Also over time while a cell is getting
	old, it has degradation of its membranes. This degradation also leads to the release of		old, it has degradation of its membranes. This degradation also leads to the release of
-	Cytochrome C which would signal that the cell is old and ready to be killed off. Without	+	Cytochrome 'C' which would signal that the cell is old and ready to be killed off. Without
-	Cytochrome C, intrinsic apoptosis would not be possible because the apoptotic factors would	+	Cytochrome 'C', intrinsic apoptosis would not be possible because the apoptotic factors would
-	never be activated. Same as if there are mutations in ~~cytochrome~~ C causing it to be unable to	+	never be activated. Same as if there are mutations in Cytochrome 'C' causing it to be unable to
	permeate through the membrane, or if there is a mutation that increases the permeability of it		permeate through the membrane, or if there is a mutation that increases the permeability of it
	through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C		through the membrane, the apoptotic pathway would be accelerated or inhibited. (Cytochrome C
Line 55:		Line 54:

	== Purpose in ETC and Photosynthesis ==		== Purpose in ETC and Photosynthesis ==
-	Cytochrome C also plays a key role in the Electron Transport Chain in mitochondria. It is one of	+	Cytochrome 'C' also plays a key role in the Electron Transport Chain in mitochondria. It is one of
	the many electron carriers in the electron transport chain but quite a vital one. The heme group		the many electron carriers in the electron transport chain but quite a vital one. The heme group
-	portion of Cytochrome C accepts the electrons from the bc1 complex and then carries the	+	portion of Cytochrome 'C' accepts the electrons from the bc1 complex and then carries the
-	electrons to complex IV. Once at complex IV, the ~~cytochrome~~ C release their electron that they	+	electrons to complex IV. Once at complex IV, the Cytochrome 'C' release their electron that they
-	are carrying and it is given to the Cytochrome C Oxidase enzyme. This enzyme accumulates 4	+	are carrying and it is given to the Cytochrome 'C' Oxidase enzyme. This enzyme accumulates 4
	electrons and transfers them to one dioxygen		electrons and transfers them to one dioxygen
	molecule in order to make two molecules of water. It is also found within the thylakoid		molecule in order to make two molecules of water. It is also found within the thylakoid
	membrane in the chloroplast of plants and green algae. In photosynthesis,		membrane in the chloroplast of plants and green algae. In photosynthesis,
-	Cytochrome C is one of the steps that transfers electrons from photosystem II to photosystem I.	+	Cytochrome 'C' is one of the steps that transfers electrons from photosystem II to photosystem I.
	Later in the cycle, the electrochemical gradient will		Later in the cycle, the electrochemical gradient will
	then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)		then be used in order to synthesize ATP from ADP. (The Multiple Functions of Cytochrome c)
Line 69:		Line 68:
	== Medical/Research Purposes ==		== Medical/Research Purposes ==
	A proposal by many research scientists has been to regulate mitochondrial energy		A proposal by many research scientists has been to regulate mitochondrial energy
-	production and ROS production through the phosphorylation of cytochrome C. It has been	+	production and ROS production through the phosphorylation of cytochrome 'C'. It has been
-	observed that Tyr48Glu phosphomimetic mutant Cytochrome c reacts with CcO, but it is	+	observed that Tyr48Glu phosphomimetic mutant Cytochrome 'C' reacts with CcO, but it is
	partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome		partially inhibited which leads to controlled respiration. (The Multiple Functions of Cytochrome
	c) They are proposing that “this effect plays an essential role in the prevention of ROS under		c) They are proposing that “this effect plays an essential role in the prevention of ROS under
-	healthy conditions.” There is evidence when cellular stress is happening, Cytochrome C then	+	healthy conditions.” There is evidence when cellular stress is happening, Cytochrome 'C' then
	becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets		becomes phosphorylated. Once dephosphorylated, controlled respiration ceases which then sets
-	up Cytochrome C to initiate apoptosis. They report that the cellular stress causes mitochondrial	+	up Cytochrome 'C' to initiate apoptosis. They report that the cellular stress causes mitochondrial
	membrane potential differences and it needs to be taken into account to be able to determine the		membrane potential differences and it needs to be taken into account to be able to determine the
	risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of		risks behind changes in OxPhos activity. The study focuses mainly on the phosphorylation of
-	Cytochrome C, but acknowledges the fact that other factors may also be affected through their	+	Cytochrome 'C', but acknowledges the fact that other factors may also be affected through their
	actions. Others have began to focus their research on major diseases such as Huntington’s		actions. Others have began to focus their research on major diseases such as Huntington’s
	disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the		disease or diverse forms of cancer. In a post by the New Journal of Science, they report that the
	closest that anyone has come to a universal cure for cancers has been with the use of the		closest that anyone has come to a universal cure for cancers has been with the use of the
-	apoptotic function of ~~cytochrome~~ C. They went on to explain that tricking the body into	+	apoptotic function of Cytochrome 'C'. They went on to explain that tricking the body into
	believing these cancerous cells are ready to die, they could negate the effects of the ineffective		believing these cancerous cells are ready to die, they could negate the effects of the ineffective
	p53 gene.		p53 gene.