5jfc - Revision history

OCA at 12:37, 6 March 2024

2024-03-06T12:37:17Z

←Older revision		Revision as of 12:37, 6 March 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4]		[https://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The recently realized biochemical phenomenon of energy conservation through electron bifurcation provides biology with an elegant means to maximize utilization of metabolic energy. The mechanism of coordinated coupling of exergonic and endergonic oxidation-reduction reactions by a single enzyme complex has been elucidated through optical and paramagnetic spectroscopic studies revealing unprecedented features. Pairs of electrons are bifurcated over more than 1 volt of electrochemical potential by generating a low-potential, highly energetic, unstable flavin semiquinone and directing electron flow to an iron-sulfur cluster with a highly negative potential to overcome the barrier of the endergonic half reaction. The unprecedented range of thermodynamic driving force that is generated by flavin-based electron bifurcation accounts for unique chemical reactions that are catalyzed by these enzymes.
-
-	Mechanistic insights into energy conservation by flavin-based electron bifurcation.,Lubner CE, Jennings DP, Mulder DW, Schut GJ, Zadvornyy OA, Hoben JP, Tokmina-Lukaszewska M, Berry L, Nguyen DM, Lipscomb GL, Bothner B, Jones AK, Miller AF, King PW, Adams MWW, Peters JW Nat Chem Biol. 2017 Apr 10. doi: 10.1038/nchembio.2348. PMID:28394885<ref>PMID:28394885</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 5jfc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:02, 6 September 2023

2023-09-06T11:02:07Z

←Older revision		Revision as of 11:02, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='5jfc' size='340' side='right'caption='[[5jfc]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='5jfc' size='340' side='right'caption='[[5jfc]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5JFC FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JFC FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.598Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5jca\|5jca]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jfc OCA], [https://pdbe.org/5jfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jfc RCSB], [https://www.ebi.ac.uk/pdbsum/5jfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jfc ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5jfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jfc OCA], [~~http~~://pdbe.org/5jfc PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5jfc RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5jfc PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5jfc ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> <ref>PMID:7961401</ref>	+	[https://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Pyrococcus furiosus]]		[[Category: Pyrococcus furiosus]]
-	[[Category: Adams~~, M W~~]]	+	[[Category: Adams MW]]
-	[[Category: Artz~~, J H~~]]	+	[[Category: Artz JH]]
-	[[Category: King~~, P W~~]]	+	[[Category: King PW]]
-	[[Category: Lipscomb, G]]	+	[[Category: Lipscomb G]]
-	[[Category: Nguyen~~, D M~~]]	+	[[Category: Nguyen DM]]
-	[[Category: Peters~~, J W~~]]	+	[[Category: Peters JW]]
-	[[Category: Schut~~, G J~~]]	+	[[Category: Schut GJ]]
-	[[Category: Tokmina-Lukaszewska, M]]	+	[[Category: Tokmina-Lukaszewska M]]
-	[[Category: Zadvornyy~~, O A]]~~	+	[[Category: Zadvornyy OA]]
-	~~[[Category: Nfni]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 09:10, 4 December 2019

2019-12-04T09:10:49Z

←Older revision		Revision as of 09:10, 4 December 2019
Line 1:		Line 1:

	==NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==		==NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==
-	<StructureSection load='5jfc' size='340' side='right' caption='[[5jfc]], [[Resolution\|resolution]] 1.60Å' scene=''>	+	<StructureSection load='5jfc' size='340' side='right'caption='[[5jfc]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JFC FirstGlance]. <br>		<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JFC FirstGlance]. <br>
Line 24:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Pyrococcus furiosus]]		[[Category: Pyrococcus furiosus]]
	[[Category: Adams, M W]]		[[Category: Adams, M W]]

OCA at 07:31, 27 April 2017

2017-04-27T07:31:45Z

←Older revision		Revision as of 07:31, 27 April 2017
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> <ref>PMID:7961401</ref>		[[http://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> <ref>PMID:7961401</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The recently realized biochemical phenomenon of energy conservation through electron bifurcation provides biology with an elegant means to maximize utilization of metabolic energy. The mechanism of coordinated coupling of exergonic and endergonic oxidation-reduction reactions by a single enzyme complex has been elucidated through optical and paramagnetic spectroscopic studies revealing unprecedented features. Pairs of electrons are bifurcated over more than 1 volt of electrochemical potential by generating a low-potential, highly energetic, unstable flavin semiquinone and directing electron flow to an iron-sulfur cluster with a highly negative potential to overcome the barrier of the endergonic half reaction. The unprecedented range of thermodynamic driving force that is generated by flavin-based electron bifurcation accounts for unique chemical reactions that are catalyzed by these enzymes.
		+
		+	Mechanistic insights into energy conservation by flavin-based electron bifurcation.,Lubner CE, Jennings DP, Mulder DW, Schut GJ, Zadvornyy OA, Hoben JP, Tokmina-Lukaszewska M, Berry L, Nguyen DM, Lipscomb GL, Bothner B, Jones AK, Miller AF, King PW, Adams MWW, Peters JW Nat Chem Biol. 2017 Apr 10. doi: 10.1038/nchembio.2348. PMID:28394885<ref>PMID:28394885</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5jfc" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:43, 12 April 2017

2017-04-12T11:43:18Z

←Older revision		Revision as of 11:43, 12 April 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5jfc ~~is ON HOLD until Paper Publication~~	+	==NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus==
-		+	<StructureSection load='5jfc' size='340' side='right' caption='[[5jfc]], [[Resolution\|resolution]] 1.60Å' scene=''>
-	~~Authors~~: ~~Zadvornyy~~, O.A., ~~Schut~~, G.J., ~~Nguyen~~, D.M., ~~Artz~~, J.H., ~~Tokmina~~-~~Lukaszewska~~, M., ~~Lipscomb~~, G., ~~King~~, P.W., ~~Adams~~, ~~M.W~~., ~~Peters~~, J.W.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5jfc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JFC FirstGlance]. <br>
-	~~Description~~: ~~NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from~~ Pyrococcus furiosus	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5jca\|5jca]]</td></tr>
-	[[Category: ~~Nguyen~~, ~~D.M~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(ferredoxin) NAD(P)(+) transhydrogenase (ferredoxin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.4 1.6.1.4] </span></td></tr>
-	[[Category: ~~Schut~~, ~~G.J~~]]	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jfc OCA], [http://pdbe.org/5jfc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jfc RCSB], [http://www.ebi.ac.uk/pdbsum/5jfc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jfc ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SUDHA_PYRFU SUDHA_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> [REFERENCE:4] [[http://www.uniprot.org/uniprot/SUDHB_PYRFU SUDHB_PYRFU]] A bifunctional enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide with NADPH as electron donor. Also functions as a reduced ferredoxin:NADP oxidoreductase with a very high affinity for reduced ferredoxin. Exhibits a broad specificity for various physiological and non-physiological substrates with varied reduction potentials such as methyl viologen, benzyl viologen, FAD, FMN, methylene blue, 2,6-dichlorophenolindophenol (DCIP), cytochrome C and ferricyanide with highest preference for benzyl viologen. Does not reduce fumarate, succinate, nitrate, nitrite, sulfate, sulfite or protons. Does not possess any hydrogenase activity or NADPH-dependent glutamate synthase activity.<ref>PMID:10968624</ref> <ref>PMID:7961401</ref> <ref>PMID:7961401</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Pyrococcus furiosus]]
		+	[[Category: Adams, M W]]
		+	[[Category: Artz, J H]]
		+	[[Category: King, P W]]
	[[Category: Lipscomb, G]]		[[Category: Lipscomb, G]]
-	[[Category: ~~King, P.W]]~~	+	[[Category: Nguyen, D M]]
-	~~[[Category: Adams~~, M.W]]	+	[[Category: Peters, J W]]
-	[[Category: Peters, J.W]]	+	[[Category: Schut, G J]]
-	[[Category: ~~Zadvornyy, O.A]]~~	+
-	~~[[Category: Artz~~, J.H]]	+
	[[Category: Tokmina-Lukaszewska, M]]		[[Category: Tokmina-Lukaszewska, M]]
		+	[[Category: Zadvornyy, O A]]
		+	[[Category: Nfni]]
		+	[[Category: Oxidoreductase]]

OCA at 09:51, 9 March 2017

2017-03-09T09:51:58Z

←Older revision		Revision as of 09:51, 9 March 2017
Line 7:		Line 7:
	Description: NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus		Description: NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Adams, M.W]]
-	[[Category: Peters, J.W]]
-	[[Category: Artz, J.H]]
	[[Category: Nguyen, D.M]]		[[Category: Nguyen, D.M]]
	[[Category: Schut, G.J]]		[[Category: Schut, G.J]]
	[[Category: Lipscomb, G]]		[[Category: Lipscomb, G]]
	[[Category: King, P.W]]		[[Category: King, P.W]]
		+	[[Category: Adams, M.W]]
		+	[[Category: Peters, J.W]]
	[[Category: Zadvornyy, O.A]]		[[Category: Zadvornyy, O.A]]
		+	[[Category: Artz, J.H]]
	[[Category: Tokmina-Lukaszewska, M]]		[[Category: Tokmina-Lukaszewska, M]]

OCA at 13:16, 9 September 2016

2016-09-09T13:16:13Z

←Older revision		Revision as of 13:16, 9 September 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5jfc is ON HOLD	+	The entry 5jfc is ON HOLD until Paper Publication

	Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., King, P.W., Adams, M.W., Peters, J.W.		Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., King, P.W., Adams, M.W., Peters, J.W.

OCA at 12:42, 20 June 2016

2016-06-20T12:42:18Z

←Older revision		Revision as of 12:42, 20 June 2016
Line 3:		Line 3:
	The entry 5jfc is ON HOLD		The entry 5jfc is ON HOLD

-	Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W.	+	Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., King, P.W., Adams, M.W., Peters, J.W.

	Description: NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus		Description: NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
Line 13:		Line 13:
	[[Category: Schut, G.J]]		[[Category: Schut, G.J]]
	[[Category: Lipscomb, G]]		[[Category: Lipscomb, G]]
		+	[[Category: King, P.W]]
	[[Category: Zadvornyy, O.A]]		[[Category: Zadvornyy, O.A]]
	[[Category: Tokmina-Lukaszewska, M]]		[[Category: Tokmina-Lukaszewska, M]]

OCA: Protected "5jfc" [edit=sysop:move=sysop]

2016-05-11T01:57:36Z

Protected "5jfc" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:57, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5jfc is ON HOLD Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W. D...

2016-05-11T01:57:35Z

New page: '''Unreleased structure''' The entry 5jfc is ON HOLD Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W. D...

New page

'''Unreleased structure'''

The entry 5jfc is ON HOLD

Authors: Zadvornyy, O.A., Schut, G.J., Nguyen, D.M., Artz, J.H., Tokmina-Lukaszewska, M., Lipscomb, G., Adams, M.W., Peters, J.W.

Description: NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
[[Category: Unreleased Structures]]
[[Category: Adams, M.W]]
[[Category: Peters, J.W]]
[[Category: Artz, J.H]]
[[Category: Nguyen, D.M]]
[[Category: Schut, G.J]]
[[Category: Lipscomb, G]]
[[Category: Zadvornyy, O.A]]
[[Category: Tokmina-Lukaszewska, M]]