Sandbox Reserved 335

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== Function ==
== Function ==
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Monoheme cytochromes ''c'' are involved in electron transport chains in both prokaryotes and eukaryotic mitochondria. They mediate the transfer of electrons mainly from the ''bc''<sub>1</sub> complexes, or their analogs, in the electron transport chain to heme-copper oxygen reductases (HCOs)<ref>PMID:11334784</ref> during oxidative phosphorylation.
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Monoheme cytochromes ''c'' are involved in electron transport chains in both prokaryotes and eukaryotic mitochondria.<ref name=main /> They mediate the transfer of electrons mainly from the ''bc''<sub>1</sub> complexes, or their analogs, in the electron transport chain to heme-copper oxygen reductases (HCOs) during oxidative phosphorylation.
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The heme ''c'' containing domains are often found fused to other protein domains, including those in the ''caa''<sub>3</sub> oxygen reductases; these enzymes are membrane-bound and catalyze the reduction of O<sub>2</sub> to water.<ref>DOI:10.1007/s00775-003-0509-9</ref>
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The heme ''c'' containing domains are often found fused to other protein domains, including those in the ''caa''<sub>3</sub> oxygen reductases<ref name=main /><ref>PMID:14691678</ref>; these enzymes are membrane-bound and catalyze the reduction of O<sub>2</sub> to water.<ref>DOI:10.1007/s00775-003-0509-9</ref>

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PDB ID 3cp5

Drag the structure with the mouse to rotate
3cp5, resolution 1.24Å ()
Ligands: ,
Gene: cytC (Rhodothermus marinus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Cytochrome c (cyt c) is a superfamily of proteins belonging to the class of all-α proteins with a core of helices and a covalently-bound heme prosthetic group.[1][2] The cytochrome c superfamily contains many different families including monodomain and multi-domain C-type cytochromes (ex. cyt c4, a two-domain C-type cytochrome, and NrfB, a pentaheme C-type cytochrome). This page focuses mainly on the cytochrome c superfamily, briefly discussing various types within the superfamily. The monoheme cytochrome c purified from Rhodothermus marinus will be discussed in greater detail than other C-type cytochromes.

Contents

Introduction

Rhodothermus marinus

Function

Monoheme cytochromes c are involved in electron transport chains in both prokaryotes and eukaryotic mitochondria.[2] They mediate the transfer of electrons mainly from the bc1 complexes, or their analogs, in the electron transport chain to heme-copper oxygen reductases (HCOs) during oxidative phosphorylation. The heme c containing domains are often found fused to other protein domains, including those in the caa3 oxygen reductases[2][3]; these enzymes are membrane-bound and catalyze the reduction of O2 to water.[4]


Structure

All members in the C-type cytochrome superfamily contain a heme prosthetic group that is covalently attached to the protein via two thioether bonds to cysteine residues.[2] Most cytochromes c occur in a CXXCH motif, where a histidine residue is one of the two axial ligands of the heme iron. The other axial position may be left vacant or be occupied mostly by histidine or methionine residues, but can sometimes be occupied by cysteine or leucine residues.[2]

Rhodothermus marinus monoheme cytochrome c

The typical monoheme cyt c fold is formed by helices .



Mechanism

Importance

References

Yay bacteria!!! [5]

  1. ↑ Gough J, Karplus K, Hughey R, Chothia C. Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J Mol Biol. 2001 Nov 2;313(4):903-19. PMID:11697912 doi:10.1006/jmbi.2001.5080
  2. ↑ 2.0 2.1 2.2 2.3 2.4 Stelter M, Melo AM, Pereira MM, Gomes CM, Hreggvidsson GO, Hjorleifsdottir S, Saraiva LM, Teixeira M, Archer M. A Novel Type of Monoheme Cytochrome c: Biochemical and Structural Characterization at 1.23 A Resolution of Rhodothermus marinus Cytochrome c. Biochemistry. 2008 Oct 15. PMID:18855424 doi:10.1021/bi800999g
  3. ↑ Soares CM, Baptista AM, Pereira MM, Teixeira M. Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase. J Biol Inorg Chem. 2004 Mar;9(2):124-34. Epub 2003 Dec 23. PMID:14691678 doi:10.1007/s00775-003-0509-9
  4. ↑ Soares CM, Baptista AM, Pereira MM, Teixeira M. Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase. J Biol Inorg Chem. 2004 Mar;9(2):124-34. Epub 2003 Dec 23. PMID:14691678 doi:10.1007/s00775-003-0509-9
  5. ↑ Alfredsson GA, Kristjansson JK, Hjörleifsdottir S, Stetter, KO. Rhodothermus marinus, gen. nov., sp. nov., a thermophilic, halophilic bacterium from submarine hot springs in Iceland. J Gen Microbiol. 1988 Feb;134(2):299-306.
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