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<StructureSection load='3cp5' size='400' side='right' scene='Cytochrome_c/Cyt_c/1' caption='Cytochrome c with heme complex with sulfate (PDB code [[3cp5]])'>
<StructureSection load='' size='350' side='right' scene='Cytochrome_c/Cyt_c/1' caption='Cytochrome c with heme complex with sulfate (PDB code [[3cp5]])'>
The '''cytochrome ''c''''' (cyt ''c'') proteins are a superfamily belonging to the class of [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins], which are denoted as such by having an α-helical core. Each protein in this superfamily also contains one or more covalently-bound [http://en.wikipedia.org/wiki/Heme heme prosthetic groups].<ref>PMID:11697912</ref><ref name=main /> The cyt ''c'' superfamily contains many different families, some of which are better characterized than others. These families include monodomain and multi-domain C-type cytochromes, such as [http://proteopedia.org/wiki/index.php/1etp cyt c4], a diheme C-type cytochrome, and [http://proteopedia.org/wiki/index.php/2ozy NrfB], a pentaheme C-type cytochrome. In particular, the monoheme cyt ''c'' from ''Rhodothermus marinus'' has been previously studied and provides an excellent example of how some protein characteristics and structures can be extremely diverse, yet conserved, through evolution.  For details on decaheme cyt see [[MtrF]].
The '''cytochrome ''c''''' (cyt ''c'') proteins are a superfamily belonging to the class of [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins], which are denoted as such by having an α-helical core. Each protein in this superfamily also contains one or more covalently-bound [http://en.wikipedia.org/wiki/Heme heme prosthetic groups].<ref>PMID:11697912</ref><ref name=main /> The cyt ''c'' superfamily contains many different families, some of which are better characterized than others. These families include monodomain and multi-domain C-type cytochromes, such as [http://proteopedia.org/wiki/index.php/1etp cyt c4], a diheme C-type cytochrome, and [http://proteopedia.org/wiki/index.php/2ozy NrfB], a pentaheme C-type cytochrome. In particular, the monoheme cyt ''c'' from ''Rhodothermus marinus'' has been previously studied and provides an excellent example of how some protein characteristics and structures can be extremely diverse, yet conserved, through evolution.<br /> For details on decaheme cyt see [[MtrF]].<br /> 
 
Cytochromes c549, c550, c553, c554, c555, c556, c557, c558, c562 are named after their optical absorption band length.
 
*'''Cytochrome c2''' transfers electron from the reduced heme to the bacteriochlorophyl in the reaction centre<ref> PMID 15977062</ref>.
*'''Cytochrome c3''' is specific to anaerobic metabolism in sulphate-reducing bacteria<ref> PMID 12885397</ref>.
*'''Cytochrome c4''' is a dihaem cytochrome<ref> PMID 9032080</ref>.
*'''Cytochrome c7''' is a tri-haem cytochrome<ref> PMID 15133162</ref>.  For details on Cyt c7 see [[Cytochrome c 7]].
*'''Cytochrome c550''' is a component of the PSII complex of cyanobacteria<ref> PMID 22289879</ref>.
*'''Cytochrome c553''' is the primary electron donor of the heliobacteria reaction centre<ref> PMID 24557489</ref>.
*'''Cytochrome c554''' is a tetra-haem cytochrome involved in the oxidation of ammonia<ref> PMID 11372197</ref>.
*'''Cytochrome c555''' is a cytochrome from a primitive anaerobic green sulphur bacteria<ref> PMID 202947</ref>.
*'''Cytochrome c557''' and '''cytochrome c558''' are mitochondrial and contain atypical harm-binding sitei<ref> PMID 242319</ref>.
*'''Cytochrome cL''' is found in methylotrops.  It receives an electron from PQQ cofactor of methanol dehydrogenase to produce formaldehyde<ref> PMID 32627749</ref>.
*'''Cytochrome cd1''' icatalyzes the reduction of NO2 to NO and water.
*'''Cytochrome cH''' is the electron donor to the oxidase in methylotrophs<ref> PMID 10386873</ref>.
*'''Cytochrome c XoxG''' is a cytochrome from the lanthanide-dependent methanol dehydrogenase system of methylothrophic bacteria<ref> PMID 31017712</ref>.
See also [[Cytochrome C -Adis]], [[Hemeproteins]], [[Cytochrome C (Hebrew)]], [[Cytochrome C (arabic)]].


== Introduction ==
== Introduction ==
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<scene name='Sandbox_Reserved_335/Heme/1'>'Figure 1. The heme group of monoheme cytochrome ''c'' purified from ''Rhodothermus marinus''</scene>
<scene name='Sandbox_Reserved_335/Heme/1'>'Figure 1. The heme group of monoheme cytochrome ''c'' purified from ''Rhodothermus marinus''</scene>


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. Most cytochromes ''c'' occur in a <scene name='Sandbox_Reserved_335/Motif/1'>CXXCH motif</scene> where the histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> In monoheme cytochromes ''c'', the other axial position may be left vacant or be occupied by histidine or methionine residues; however, it can sometimes be occupied by cysteine or lysine residues.<ref name=main />. In ''Rm''cyt''c'', XX represents a threonine (Thr46) and an alanine residue (Ala47) that help form the loop 2 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. Most cytochromes ''c'' occur in a where the histidine residue is one of the two axial ligands of the heme iron.<ref name=main>PMID:18855424</ref><ref name=heme /> In monoheme cytochromes ''c'', the other axial position may be left vacant or be occupied by histidine or methionine residues; however, it can sometimes be occupied by cysteine or lysine residues.<ref name=main />. In ''Rm''cyt''c'', XX represents a threonine (Thr46) and an alanine residue (Ala47) that help form the loop 2 structure.


[[Image:heme.gif |frame|left| Figure 2. The tetrapyrrolic heme prosthetic group that can either be covalently attached to or closely associated with various proteins, such as cytochromes and other globin proteins. In ''Rm''cyt''c'', R2 is an ethyl group covalently attached to Cys 45, and R3 is a methyl group covalently attached to Cys48.]]
[[Image:heme.gif |frame|left| Figure 2. The tetrapyrrolic heme prosthetic group that can either be covalently attached to or closely associated with various proteins, such as cytochromes and other globin proteins. In ''Rm''cyt''c'', R2 is an ethyl group covalently attached to Cys 45, and R3 is a methyl group covalently attached to Cys48.]]
 
{{Clear}}
The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/4'>A, C, and E</scene>. ''Rm''cyt''c'' contains seven α-helices that are folded around the heme, all connected by random coils.<ref name=main /> The heme group is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/6'>His49 and Met100</scene>, and the disulfide linkages exist at <scene name='Sandbox_Reserved_335/Cys/1'>Cys45 and Cys48</scene>. The heme group in ''Rm''cyt''c'' is almost completely shielded from solvent due to it being in a mostly hydrophobic pocket. This pocket is formed in part by the seven helices surrounding the ring, but also by two structures that are uncommon in other cytochromes ''c''. First, a 21 amino acid extension of the N-terminal exists, forming <scene name='Sandbox_Reserved_335/Uncommon1/2'>α-helix A' and loop 1</scene>, which wraps around the back of the polypeptide.<ref name=main /> An extension resembling such has only been seen in ''Thermus thermophilus''; however, the extension occurs at the C-terminus rather than the N-terminus.<ref>doi:10.1006/jmbi.1997.1181</ref> A second rarity is that of <scene name='Sandbox_Reserved_335/Uncommon2/2'>helix B'</scene>, inserted between helix D and loop 3, that shields the bottom part of the heme from any solvent.<ref name=main /> In cytochrome ''c''<sub>2</sub> as well as mitochondrial cyt ''c'', a similar yet shorter helix was found, though this helix was present at a different place in the primary sequence. Also, instead of helix B', ''T. thermophilus'' contains a two-stranded [http://en.wikipedia.org/wiki/Beta_sheet β-sheet].<ref name=main /> One final note is the number of <scene name='Sandbox_Reserved_335/Met/1'>methionine</scene> residues that ''Rm''cyt''c'' contains. In general, cyt ''c'' contains about two methionines whereas ''Rm''cyt''c'' contains seven, located on the left of the heme.<ref name=main />
The typical monoheme cyt ''c'' fold is formed by helices <scene name='Sandbox_Reserved_335/Helices/4'>A, C, and E</scene>. ''Rm''cyt''c'' contains seven α-helices that are folded around the heme, all connected by random coils.<ref name=main /> The heme group is axially coordinated by <scene name='Sandbox_Reserved_335/Axial/6'>His49 and Met100</scene>, and the disulfide linkages exist at <scene name='Sandbox_Reserved_335/Cys/1'>Cys45 and Cys48</scene>. The heme group in ''Rm''cyt''c'' is almost completely shielded from solvent due to it being in a mostly hydrophobic pocket. This pocket is formed in part by the seven helices surrounding the ring, but also by two structures that are uncommon in other cytochromes ''c''. First, a 21 amino acid extension of the N-terminal exists, forming <scene name='Sandbox_Reserved_335/Uncommon1/2'>α-helix A' and loop 1</scene>, which wraps around the back of the polypeptide.<ref name=main /> An extension resembling such has only been seen in ''Thermus thermophilus''; however, the extension occurs at the C-terminus rather than the N-terminus.<ref>doi:10.1006/jmbi.1997.1181</ref> A second rarity is that of <scene name='Sandbox_Reserved_335/Uncommon2/2'>helix B'</scene>, inserted between helix D and loop 3, that shields the bottom part of the heme from any solvent.<ref name=main /> In cytochrome ''c''<sub>2</sub> as well as mitochondrial cyt ''c'', a similar yet shorter helix was found, though this helix was present at a different place in the primary sequence. Also, instead of helix B', ''T. thermophilus'' contains a two-stranded [http://en.wikipedia.org/wiki/Beta_sheet β-sheet].<ref name=main /> One final note is the number of <scene name='Sandbox_Reserved_335/Met/1'>methionine</scene> residues that ''Rm''cyt''c'' contains. In general, cyt ''c'' contains about two methionines whereas ''Rm''cyt''c'' contains seven, located on the left of the heme.<ref name=main />


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== Electron transport chain ==
== Electron transport chain ==


In the electron transport chain (ETC), cyt ''c'' shuttles electrons between the respiratory complexes III and IV; complex III is the cytochrome ''bc''<sub>1</sub> complex and IV is cyt ''c'' oxidase. Initially, the heme iron in cyt ''c'' is in the reduced, Fe<sup>3+</sup> state; this allows for the uptake of one electron, oxidizing the iron to the Fe<sup>2+</sup> state.<ref name='etc'>Karp, Gerald (2008). Cell and Molecular Biology (5th edition). Hoboken, NJ: John Wiley & Sons. ISBN 978-0470042175.</ref> The ETC in eukaryotes is quite simple compared to that of prokaryotes (Figure 3). [[Image:Etc.gif |frame|left| |size|300| Figure 3. The electron transport chain of a) eukaryotes as compared to b) prokaryotes.]] In prokaryotic systems, electrons can enter the ETC at a number of places and multiple donors can be in play; however, the underlying transport system remains the same. Electrons are ultimately transferred from donor to various redox complexes including the ''bc''<sub>1</sub> complex and cytochrome ''c'', and finally to a terminal electron acceptor such as molecular oxygen in eukaryotes.<ref name=etc />
In the electron transport chain (ETC), cyt ''c'' shuttles electrons between the respiratory complexes III and IV; complex III is the cytochrome ''bc''<sub>1</sub> complex and IV is cyt ''c'' oxidase. Initially, the heme iron in cyt ''c'' is in the reduced, Fe<sup>3+</sup> state; this allows for the uptake of one electron, oxidizing the iron to the Fe<sup>2+</sup> state.<ref name='etc'>Karp, Gerald (2008). Cell and Molecular Biology (5th edition). Hoboken, NJ: John Wiley & Sons. ISBN 978-0470042175.</ref> The ETC in eukaryotes is quite simple compared to that of prokaryotes (Figure 3).  
[[Image:Etc.gif |frame|left|thumb|300px| Figure 3. The electron transport chain of a) eukaryotes as compared to b) prokaryotes.]]  
 
In prokaryotic systems, electrons can enter the ETC at a number of places and multiple donors can be in play; however, the underlying transport system remains the same. Electrons are ultimately transferred from donor to various redox complexes including the ''bc''<sub>1</sub> complex and cytochrome ''c'', and finally to a terminal electron acceptor such as molecular oxygen in eukaryotes.<ref name=etc />


The cytochrome oxidase reaction accounts for nearly 90% of all oxygen uptake in most cells.<ref name=etc /> Due to the large role of cytochromes within the ETC, it would be highly detrimental to the cell if any inhibitors were to be present in the organism. Cyanide and azide bind tightly to the cytochrome oxidase complex, halting electron transport and reducing the overall ATP production.<ref name=etc />
The cytochrome oxidase reaction accounts for nearly 90% of all oxygen uptake in most cells.<ref name=etc /> Due to the large role of cytochromes within the ETC, it would be highly detrimental to the cell if any inhibitors were to be present in the organism. Cyanide and azide bind tightly to the cytochrome oxidase complex, halting electron transport and reducing the overall ATP production.<ref name=etc />
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==Structural model of the [Fe]-hydrogenase/cytochrome C553 complex combining NMR and soft-docking<ref>PMID:10748163</ref>==
==Structural model of the [Fe]-hydrogenase/cytochrome C553 complex combining NMR and soft-docking<ref>PMID:10748163</ref>==
The <scene name='1e08/1e08-cofactors/1'>complex</scene> shows the specific interaction of the hydrogenase (light blue) with the cytochrome (pink), revealing the path of electron transport from the <scene name='1e08/1e08-activecluster/3'>active site metal cluster</scene>, through three iron-sulfur clusters, and ending in the cytochrome heme (colored red). Two <scene name='1e08/1e08-cys/2'>cysteine amino acids at the interface</scene>, CYS 38 in the hydrogenase and CYS10 in the cytochrome, are thought to provide the electron transfer pathway between the two proteins (these scenes were created by Jaime Prilusky, David S. Goodsell, and Eran Hodis).
The <scene name='1e08/1e08-cofactors/1'>complex</scene> shows the specific interaction of the hydrogenase (light blue) with the cytochrome (pink), revealing the path of electron transport from the <scene name='1e08/1e08-activecluster/3'>active site metal cluster</scene>, through three iron-sulfur clusters, and ending in the cytochrome heme (colored red). Two <scene name='1e08/1e08-cys/2'>cysteine amino acids at the interface</scene>, CYS 38 in the hydrogenase and CYS10 in the cytochrome, are thought to provide the electron transfer pathway between the two proteins (these scenes were created by Jaime Prilusky, David S. Goodsell, and Eran Hodis).
</StructureSection>


==3D structures of cytochrome C==
== Conformational control of the binding of diatomic gases to cytochrome c’ <ref>PMID 25792378 </ref>==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
The cytochromes c′ (CYTcp) are found in denitrifying, methanotrophic and photosynthetic bacteria. These proteins are able to form stable adducts with CO and NO but not with O2. The binding of NO to CYTcp currently provides the best structural model for the NO activation mechanism of soluble guanylate cyclase. Ligand binding in CYTcps has been shown to be highly dependent on residues in both the proximal and distal heme pockets. Group 1 CYTcps typically have a phenylalanine residue positioned close to the distal face of heme, while for group 2, this residue is typically leucine. We have structurally, spectroscopically and kinetically characterised the CYTcp from ''Shewanella frigidimarina'' <scene name='69/696899/Cv/2'>(SFCP)</scene>, a protein that has a distal phenylalanine residue and a lysine in the proximal pocket in place of the more common arginine (<font color='red'><b>monomer A is colored in red</b></font>, <span style="color:lime;background-color:black;font-weight:bold;">monomer B in green</span>, and <span style="color:yellow;background-color:black;font-weight:bold;">heme group in yellow</span>). <scene name='69/696899/Cv/3'>Each monomer of the SFCP dimer folds as a 4-alpha-helical bundle</scene> in a similar manner to CYTcps previously characterised.
{{#tree:id=OrganizedByTopic|openlevels=0|
* <scene name='69/696899/Cv/4'>Heme group and its environment in as-isolated SFCP</scene>.
* <scene name='69/696899/Cv/5'>Proximal NO complex of SFCP (monomer A)</scene>.
* <scene name='69/696899/Cv/8'>Click here to see the difference between these structures</scene>.
SFCP exhibits biphasic binding kinetics for both NO and CO as a result of the high level of steric hindrance from the aromatic side chain of residue Phe 16. The binding of distal ligands is thus controlled by the conformation of the phenylalanine ring.
* <scene name='69/696899/Cv/12'>A superposition of the heme environments</scene> of <span style="color:lime;background-color:black;font-weight:bold;">SFCP (in green</span>;[[4ulv]]), <font color='magenta'><b>RCCP (''R. capsulatus''; in magenta</b></font>; [[1cpq]]), <font color='red'><b>RSCP (''R. sphaeroides''; in red</b></font>; [[1gqa]]) and <span style="color:cyan;background-color:black;font-weight:bold;">RGCP (''R. gelatinosus''; in cya)</span>; [[2j8w]]).
* <scene name='69/696899/Cv/14'>Click here to see morph of this scene</scene>.
Only a proximal 5-coordinate NO adduct, confirmed by structural data, is observed with no detectable hexacoordinate distal NO adduct.


*Cytochrome C
==3D structures of cytochrome C==
[[Cytochrome C 3D structures]]


**[[3nwv]], [[3zoo]] – hCyt (mutant) – human<BR />
</StructureSection>
**[[3zcf]] – hCyt<br />
**[[1j3s]] – hCyt - NMR<BR />
**[[3nbs]], [[3nbt]], [[1crc]], [[1hrc]], [[3o1y]], [[3o20]], [[3wc8]], [[3wui]], [[4rsz]] – hoCyt – horse<BR />
**[[1lc1]], [[1lc2]], [[1m60]], [[1giw]], [[2giw]], [[1akk]], [[2frc]], [[1ocd]] – hoCyt – NMR<BR />
**[[1fi9]], [[1fi7]] - hoCyt + imidazole – NMR<BR />
**[[1u75]] - hoCyt + Cyt peroxidase<BR />
**[[1wej]] – hoCyt + Fab fragment<BR />
**[[3a9f]] – CtCyt C-terminal – ''Chlorobaculum tepidum''<BR />
**[[3cp5]] – Cyt residues 29-152 – ''Rhodothermus marinus''<BR />
**[[2jti]], [[3tyi]] – yCyt (mutant) + Cyt peroxidase – yeast<BR />
**[[2pcb]] - yCyt + Cyt peroxidase<BR />
**[[2gb8]] - yCyt + Cyt peroxidase - NMR<BR />
**[[2jqr]] - yCyt (mutant) + adrenodoxin<BR />
**[[2orl]] - yCyt (mutant) – NMR<BR />
**[[1crg]], [[1crh]], [[1cri]], [[1crj]], [[ 2ycc]] - yCyt<BR />
**[[1ytc]], [[1cie]], [[1cif]], [[1cig]], [[1cih]], [[1csu]], [[1csv]], [[1csw]], [[1csx]], [[1chh]], [[1chi]], [[1chj]], [[1cty]], [[1ctz]] - yCyt (mutant)<br />
**[[1rap]], [[1raq]], [[1ycc]]- yCyt iso-1<BR />
**[[1yic]] – yCyt iso-1 – NMR<BR />
**[[1irv]], [[1irw]], [[1lms]], [[4mu8]], [[4n0k]] – yCyt iso-1 (mutant) <BR />
**[[2hv4]], [[2lir]], [[2lit]], [[2mhm]] - yCyt iso-1 (mutant) - NMR<br />
**[[1fhb]] - yCyt iso-1 (mutant) + CN - NMR<BR />
**[[1nmi]] – yCyt iso-1 + imidazole<BR />
**[[2b0z]], [[2b10]], [[2b11]], [[2b12]], [[1u74]], [[1s6v]], [[2bcn]] – yCyt iso-1 (mutant) + Cyt peroxidase<BR />
**[[2pcc]] – yCyt iso-1 + Cyt peroxidase<BR />
**[[1yea]], [[1yeb]] – yCyt iso-2<BR />
**[[2e84]] – DvCyt – ''Desulfovibrio vulgaris''<BR />
**[[2j7a]] – DvCyt catalytic + electron donor subunits<BR />
**[[2oz1]] – RsuCyt – ''Rhodovulum sulfidophilum''<BR />
**[[1h31]], [[1h32]], [[1h33]] – RsuCyt diheme<br />
**[[2aiu]] – Cyt – mouse<BR />
**[[2fw5]], [[2fwt]] – RsCyt diheme residues 1-139 - ''Rhodobacter sphaeroides''<BR />
**[[1dw0]], [[1dw3]] - RsCyt diheme residues 1-112<BR />
**[[1dw1]], [[1dw2]] - RsCyt diheme residues 1-112 + small molecule<BR />
**[[1ogy]] - RsCyt diheme residues 25-154 + nitrate reductase catalytic subunit<BR />
**[[2a3m]], [[2a3p]] – DdCyt tetraheme membrane-bound subunit - ''Desulfovibrio desulfuricans''<BR />
**[[1h21]] - DdCyt di-heme<BR />
**[[1ofw]], [[1ofy]], [[1duw]], [[19hc]] - DdCyt nine-heme<BR />
**[[1oah]] - DdCyt<BR />
**[[2b4z]] – bCyt – bovine<BR />
**[[1lfm]], [[1i55]], [[3cyt]], [[1i54]], [[1i5t]] -  Cyt – tuna<BR />
**[[1fs7]], [[1fs8]], [[1fs9]] – WsCyt + small molecule – ''Wolinella succinogenes''<BR />
**[[1dxr]] – RvCyt in photosynthetic reaction center – ''Rhodopseudomonas viridis''<BR />
**[[1qdb]] – Cyt – ''Sulfurospirillum deleyianum''<BR />
**[[5cyt]] – Cyt - albacore<br />
**[[2ccy]] – Cyt – ''Phaeospirillum molischianum''<br />
**[[4dy9]] – Cyt – ''Leishmania major''<br />
**[[3u99]] – Cyt diheme – ''Shewanella baltica''<br />
**[[3j2t]] – Cyt + apoptotic protease-activating factor 1 – bovine – Cryo EM<br />
 
*Cytochrome C’
 
**[[2xl6]], [[2xld]], [[2xle]], [[2xlo]], [[2xlv]], [[2xlw]] – AxCyt (mutant) + NO – ''Achromobacter xylosoxidans''<BR />
**[[1cgn]], [[1cgo]], [[2ykz]], [[3zqv]], [[2yli]], [[4cda]], [[4cdv]], [[4cdy]], [[4cip]], [[4cjo]], [[4wgy]], [[4wgz]] - AxCyt<BR />
**[[2xm0]], [[2xm4]], [[2xl8]], [[2xlh]], [[2yl0]], [[2yl7]], [[3ztm]] - AxCyt (mutant) <BR />
**[[2yl1]], [[2yl3]], [[2ylg]], [[3zqy]], [[3ztz]] - AxCyt (mutant) + CO<br />
**[[2yld]], [[3zwi]] - AxCyt + CO<br />
**[[2xlm]], [[4cjg]] - AxCyt + NO<BR />
**[[2j9b]], [[2j8w]] – Cyt – ''Rubrivivax gelatinosus''<BR />
**[[1gqa]] – RsCyt<BR />
**[[1mqv]], [[1a7v]] – RpCyt – ''Rhodopseudomonas palustris''<BR />
**[[1eky]] – RcCyt]] - ''Rhodobacter capsulatus'' – NMR<BR />
**[[1cpr]], [[1cpq]], [[1rcp]] – RcCyt<BR />
**[[1nbb]] – RcCyt + cyanide<BR />
**[[1e83]], [[1e84]], [[1e85]], [[1e86]] – Cyt - ''Alcaligenes xylosoxidans''<BR />
**[[1jaf]] – Cyt – ''Rhodocyclus gelatinosus''<BR />
**[[1bbh]] – Cyt – ''Allochromatium vinosum''<br />
**[[3vcr]] - CtCyt<br />
**[[3vrc]] – Cyt – ''Thermochromatium tepidum''<br />
 
*Cytochrome C’’
 
**[[1oae]], [[1gu2]] – MmCyt – ''Methylophilus methylotrophus''<BR />
**[[1e8e]] – MmCyt - NMR<BR />
 
*Cytochrome C1
 
**[[3cx5]], [[3cxh]] – yCyt in complex III<BR />
**[[2ibz]] - yCyt in complex III + inhibitor<BR />
**[[1kyo]] - yCyt in Bc1 complex<BR />
**[[1kb9]] – yCyt in Bc1 complex residues 17-368<BR />
**[[1ezv]] - yCyt in Bc1 complex + antibody FV fragment<BR />
**[[3h1h]], [[1bcc]] - cCyt in Bc1 complex – chicken<BR />
**[[3h1i]], [[2bcc]], [[3bcc]] - cCyt in Bc1 complex + inhibitor<BR />
**[[2qjk]], [[2qjp]], [[2qjy]] – RsCyt in Bc1 complex + inhibitor<BR />
**[[2fyn]] - RsCyt in Bc1 complex (mutant) <BR />
**[[1l0n]], [[1be3]], [[1bgy]], [[1qcr]] – bCyt in Bc1 complex<BR />
**[[2fyu]] - bCyt in Bc1 complex (mutant) + inhibitor<BR />
**[[1sqp]], [[1sqq]], [[1sqv]], [[1sqx]], [[2a06]], [[1sqb]], [[1pp9]], [[1ppj]], [[1ntk]], [[1ntm]], [[1p84]], [[1l0l]] - bCyt in Bc1 complex + inhibitor<BR />
**[[1ntz]], [[1nu1]] - bCyt in Bc1 complex + substrate<BR />
**[[1zrt]] - RcCyt in Bc1 complex + inhibitor<br />
**[[2yiu]] - PdCyt in Bc1 complex – ''Paracoccus denitrificans''
 
*Cytochrome C2
 
**[[1c2r]] - RcCyt<BR />
**[[1vyd]] – RcCyt (mutant) <BR />
**[[1c2n]] – RcCyt - NMR<BR />
**[[1l9b]], [[1l9j]] – RsCyt in photosynthetic reaction center<BR />
**[[2cxb]], [[1cxc]], [[1cxa]] - RsCyt<BR />
**[[1jdl]] – Cyt – ''Rhodospirillum centenum''<BR />
**[[2c2c]], [[3c2c]] – Cyt – ''Rhodospirillum rubrum''<BR />
**[[1i8o]], [[1hh7]], [[1fj0]], [[1i8p]] – RpCyt<BR />
**[[1hro]] – Cyt – ''Rhodopila globiformis''<BR />
**[[1cot]] – PdCyt - ''Paracoccus denitrificans''<BR />
**[[1cry]] - RvCyt<br />
**[[1co6]], [[1io3]] – BvCyt - ''Blastochloris viridis''
 
*Cytochrome C3
 
**[[2ksu]], [[1up9]], [[1upd]], [[1gmb]], [[1gm4]], [[1i77]], [[3cyr]] – DdCyt<BR />
**[[2kmy]] – DdCyt – NMR<BR />
**[[2k3v]] – Cyt – ''Shewanella frigidimarina''<BR />
**[[1m1p]], [[1m1r]], [[1m1q]] - SoCyt tetraheme – ''Shewanella oneidensis''<BR />
**[[3pmq]] - SoCyt decaheme<br />
**[[1it1]] – DvCyt<br />
**[[2bpn]] – DvCyt fragment - NMR<br />
**[[1j0o]], [[2cth]], [[2cdv]] - DvCyt tetraheme<BR />
**[[2z47]], [[2yyw]], [[2yyx]], [[2yxc]], [[2ffn]], [[2ewi]], [[2ewk]], [[2ewu]], [[1wr5]], [[1j0p]], [[1mdv]], [[2cym]] – DvCyt tetraheme (mutant) <BR />
**[[1gx7]] – DvCyt + hydrogenase<BR />
**[[1gyo]], [[1wad]], [[1qn0]], [[1qn1]] - DgCyt di-tetraheme – ''Desulfovibrio gigas''<BR />
**[[1z1n]] - DgCyt sixteen heme<br />
**[[2bq4]], [[3cao]], [[3car]] – Cyt – ''Desulfovibrio africanus''<BR />
**[[1w7o]] - Cyt – ''Desulfomicrobium baculatus''<BR />
**[[1aqe]] – DnCyt (mutant) – ''Desulfomicrobium norvegicum''<br />
**[[1czj]], [[2cy3]] - DnCyt<br />
**[[1a2i]] - DvCyt<br />
**[[2ldo]] – GsCyt residues 21-91 – ''Geobacter sulfurreducens'' - NMR<br />
**[[2izz]] - GsCyt residues 21-91 (mutant) – NMR<br />
**[[3ov0]] – GsCyt residues 26-343 dodedcaheme<br />
**[[3ouq]] - GsCyt residues 26-186 hexaheme<br />
**[[3oue]] - GsCyt residues 186-343 hexaheme
 
*Cytochrome C4
 
**[[1m6z]], [[1m70]], [[1etp]] – PsCyt – ''Pseudomonas stutzeri''<BR />
**[[1h1o]] – Cyt - ''Acidithiobacillus ferrooxidans''
 
*Cytochrome C5
 
**[[1cc5]] – Cyt – ''Azotobacter vinelandii''
 
*Cytochrome C6
 
**[[3ph2]] – PlCyt (mutant) – ''Phormidium laminosum''<BR />
**[[3dr0]], [[4eic]], [[4eie]] – SyCyt – ''Synechococcus''<BR />
**[[4eid]], [[4eif]] – SyCyt (mutant)<br />
**[[3dmi]] – Cyt – ''Phaeodactylum tricornutum''<BR />
**[[2zbo]] – Cyt – ''Hizikia fusiformis''<BR />
**[[2v07]], [[2dge]] – AtCyt residues 71-175 – ''Arabidopsis thaliana''<BR />
**[[2ce0]], [[2ce1]] - AtCyt residues 71-175 (mutant) <BR />
**[[2v08]] – PlCyt <BR />
**[[1ls9]] – Cyt – ''Cladophora glomerata''<BR />
**[[1kib]], [[1f1f ]] – AmCyt – ''Arthrospira maxima''<BR />
**[[1gdv]] – Cyt – ''Porphyra yezoensis''<BR />
**[[1a2s]], [[1ced]] – MbCyt – ''Monoraphidium braunii'' – NMR<BR />
**[[1ctj]] - MbCyt<BR />
**[[1c6s]] – Cyt – ''Cyanobacterium synechococcus'' - NMR<BR />
**[[1c6o]], [[1c6r]] – Cyt – ''Scenedesmus obliquus''<br />
**[[1ccr]] – Cyt - rice<br />
**[[4gyd]] – noCyt – nostoc<br />
**[[4h0j]], [[4h0k]] – noCyt (mutant) <br />
 
*Cytochrome C7
 
**[[3h33]], [[3h34]], [[3h4n]], [[3bxu]] – GsCyt <BR />
**[[1lm2]], [[1l3o]], [[1kwj]], [[1f22]], [[1ehj]] – DaCyt – ''Deulfurmonas acetoxidans'' – NMR<BR />
**[[1hh5]] - DaCyt
 
*Cytochrome C549
 
**[[1f1c]] – AmCyt<BR />
**[[1e29]] - SyCyt
 
*Cytochrome C550
 
**[[3arc]], [[3prq]], [[3prr]], [[3kzi]], [[3a0b]], [[3a0h]], [[3bz1]], [[3bz2]], [[1izl]] – Cyt in photosystem II – ''Thermosynechococcus vulcanus''<BR />
**[[2axt]], [[1w5c]], [[1s5l]] - TeCyt in photosystem II – ''Thermosynechococcus elongatus''<BR />
**[[2bgv]] – PvCyt – ''Paracoccus versutus''<BR />
**[[2bh4]], [[2bh5]] – PvCyt (mutant) <BR />
**[[1mz4]] – TeCyt<BR />
**[[155c]] - PdCyt
 
*Cytochrome C551
 
**[[2zon]] – AxCyt + nitrite reductase<BR />
**[[2gc7]], [[2gc4]], [[2mta]] – PdCyt + methylamine dehydrogenase + amicyanin<BR />
**[[1cch]], [[1cor]] – PsCyt - NMR<BR />
**[[1gks]] – Cyt – ''Ectothiorhodospira halophila'' - NMR<BR />
**[[1new]] – DaCyt triheme]- NMR<BR />
**[[2exv]] – PaCyt (mutant) – ''Pseudomonas aeruginosa''<BR />
**[[351c]], [[451c]] - PaCyt<BR />
**[[2pac]] – PaCyt - NMR<BR />
**[[1dvv]] - PaCyt (mutant) – NMR<BR />
**[[1fi3]], [[2i8f]] - PsCyt (mutant) – NMR
 
*Cytochrome C552 [[Nitrite reductase]]
 
*Cytochrome C553
 
**[[1b7v]], [[1c75]] – BpCyt - ''Bacillus pasteuri''<BR />
**[[1k3h]], [[1k3g]] – BpCyt – NMR<BR />
**[[1e08]] – DdCyt + hydrogenase - NMR<BR />
**[[1n9c]] – Cyt – ''Sporosarcina pasteurii''<BR />
**[[1c53]] - DvCyt<BR />
**[[1dvh]] - DvCyt - NMR<br />
**[[2dvh]] - DvCyt (mutant) - NMR<BR />
**[[1dwl]] – DvCyt + ferredoxin I – NMR<BR />
**[[1cyi]], [[1cyj]] – Cyt – ''Chlamydomonas reinhardtii''
 
*Cytochrome C554
 
**[[2zzs]] – Cyt – ''Vibrio parahaemolyticus''<BR />
**[[1ft5]], [[1ft6]], [[1bvb]] – Cyt – ''Nitrosomonas europaea''
 
*Cytochrome C555
 
**[[2zxy]] – Cyt – ''Aquifex aeolicus''<BR />
**[[2w9k]], [[2yk3]] – Cyt – ''Crithidia fasciculate''<br />
**[[4j20]] – CtCyt (mutant)<br />
 
* Cytochrome C557
 
**[[1foc]] – TtCyt – ''Thermus thermophilus''<br />
 
*Cytochrome C556
 
**[[1s05]] – RpCyt - NMR<BR />
 
*Cytochrome C558
 
**[[2x5u]], [[2x5v]] – BvCyt in photosynthetic reaction center – ''Blastochloris viridis'' – Laue<BR />
**[[2wjm]], [[2wjn]], [[3g7f]], [[3d38]], [[2jbl]], [[2i5n]], [[1vrn]], [[1r2c]] - BvCyt in photosynthetic reaction center
 
*Cytochrome C562
 
**[[3qvz]] – EcCyt + Cu + Zn
 
*Cytochrome C NAPB
 
**[[3ml1]], [[3o5a]] – Cyt + nitrate reductase catalytic subunit – ''Ralstonia eutropha''<br />
**[[1jni]] – Cyt small subunit – ''Haemophilus influenzae''
 
*Cytochrome CL
 
**[[2d0w]] – Cyt – ''Hyphomicrobium denitrificans''<BR />
**[[2c8s]] – MeCyt – ''Methylobacterium extorquens''<br />
**[[1mg2]], [[1mg3]] – PdCyt + methylamine hydrogenase + amicyanin<br />
 
*Cytochrome CC3
 
**[[2cvc]], [[1gws]], [[1h29]] – DvCyt
 
*Cytochrome CD1
 
**[[1gq1]], [[1h9x]], [[1h9y]], [[1hcm]], [[1qks]] – Cyt – ''Paracoccus pantotrophus''<BR />
**[[1gjq ]]– PaCyt<BR />
**[[1dy7]] – PaCyt + CO<BR />
**[[1e2r]] – PdCyt + CN
 
*Cytochrome CH
 
**[[1qn2]] – MeCyt
 
*Cytochrome CB562


**[[3qvy]], [[3qw0]], [[3qw1]] – EcCyt + Zn<br />
**[[3c62]], [[3c63]], [[3iq5]], [[3iq6]], [[3l1m]], [[3m15]], [[3nmi]], [[3nmk]] - EcCyt (mutant) + Zn<br />
**[[3de8]], [[3m79]] - EcCyt (mutant) + Zn + Cu<br />
**[[3de9]], [[3nmj]] - EcCyt (mutant) + Zn + Ni
}}
== References ==
== References ==


Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Melissa Morrison, Michal Harel, Alexander Berchansky, David Canner, Joel L. Sussman, Adis Hasic
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