
Ferricytochrome c (ECMDB21652) (M2MDB002046)
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Version | 2.0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Creation Date | 2012-08-15 08:51:33 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Update Date | 2015-09-17 15:41:55 -0600 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary Accession Numbers |
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Identification | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Name: | Ferricytochrome c | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Description | Cytochrome c, or Cyt c, is a small heme protein and a component of the oxidative phosphorylation electron transport chain. The heme group of cytochrome c accepts electrons from the Cytochrome b-c1 complex (Complex III) and transfers electrons to the Cytochrome oxidase complex (Complex IV). Cyt c is capable of undergoing oxidation and reduction, but does not bind oxygen. Cytochrome c is a highly conserved protein across the spectrum of species, found in plants, animals, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), makes it useful in studies of cladistics. Its primary structure consists of a chain of about 100 amino acids. (Wikipedia) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Structure | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Synonyms: |
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Chemical Formula: | C42H68O13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Weight: | Average: 780.993 Monoisotopic: 780.46599225 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
InChI Key: | FHOKVOIILRHONR-ZVBGSRNCSA-N | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
InChI: | InChI=1S/C42H68O13/c1-21(19-52-37-36(51)34(49)32(47)27(55-37)20-53-38-35(50)33(48)31(46)26(18-43)54-38)9-8-10-22(2)23-15-16-40(5)28-13-11-24-25(12-14-29(44)39(24,3)4)42(28,7)30(45)17-41(23,40)6/h9,11,22-23,25-29,31-38,43-44,46-51H,8,10,12-20H2,1-7H3/b21-9+ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
CAS number: | 9007-43-6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
IUPAC Name: | λ²-iron(2+) ion 3-[15-(1-{[2-amino-2-(methyl-C-hydroxycarbonimidoyl)ethyl]sulfanyl}ethyl)-10-(1-{[2-amino-3-(methylazanidyl)-3-oxopropyl]sulfanyl}ethyl)-20-(2-carboxyethyl)-5,9,14,19-tetramethyl-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(21),2,4,6,8,10,12,14,16(22),17,19-undecaen-4-yl]propanoate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Traditional IUPAC Name: | λ²-iron(2+) ion 3-[15-(1-{[2-amino-2-(methyl-C-hydroxycarbonimidoyl)ethyl]sulfanyl}ethyl)-10-(1-{[2-amino-3-(methylazanidyl)-3-oxopropyl]sulfanyl}ethyl)-20-(2-carboxyethyl)-5,9,14,19-tetramethyl-21,22,23,24-tetraazapentacyclo[16.2.1.1³,⁶.1⁸,¹¹.1¹³,¹⁶]tetracosa-1(21),2,4,6,8,10,12,14,16(22),17,19-undecaen-4-yl]propanoate | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SMILES: | CC(CC\C=C(/C)COC1OC(COC2OC(CO)C(O)C(O)C2O)C(O)C(O)C1O)C1CCC2(C)C3CC=C4C(CCC(O)C4(C)C)C3(C)C(=O)CC12C | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Chemical Taxonomy | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Classification | Not classified | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Physical Properties | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
State: | Solid | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Charge: | -1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Melting point: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental Properties: |
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Predicted Properties |
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Biological Properties | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Cellular Locations: | Cytoplasm | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reactions: | L-Lactic acid + 2 Ferricytochrome c + Ferricytochrome c <> Pyruvic acid +2 Ferrocytochrome c +2 Hydrogen ion + Ferrocytochrome c Ammonia + 2 Water + 6 Ferricytochrome c + Ferricytochrome c <> Nitrite +6 Ferrocytochrome c +6 Hydrogen ion + Ferrocytochrome c L-Lactic acid + 2 Ferricytochrome c > Pyruvic acid +2 Ferrocytochrome c +2 Hydrogen ion Ammonia + 2 Water + 6 Ferricytochrome c > Nitrite +6 Ferrocytochrome c +7 Hydrogen ion 2 Ferrocytochrome c + Hydrogen peroxide >2 Ferricytochrome c +2 Water Ferrocytochrome c + Hydrogen peroxide <> Ferricytochrome c + Water Nitrite + 6 ferrocytochrome c + 7 Hydrogen ion + Nitrite + 6 Ferrocytochrome c <> Ammonia +6 ferricytochrome c +2 Water +6 Ferricytochrome c L-Lactic acid + 2 Ferricytochrome c <> Pyruvic acid +2 Ferrocytochrome c +2 Hydrogen ion L-Lactic acid + 2 Ferricytochrome c <> Pyruvic acid +2 Ferrocytochrome c +2 Hydrogen ion | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
SMPDB Pathways: |
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KEGG Pathways: | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
EcoCyc Pathways: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Concentrations | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Not Available | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Spectra | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Spectra: |
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References | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
References: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Synthesis Reference: | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Material Safety Data Sheet (MSDS) | Not Available | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Links | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
External Links: |
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Enzymes
- General function:
- Involved in oxidoreductase activity
- Specific function:
- The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction
- Gene Name:
- narG
- Uniprot ID:
- P09152
- Molecular weight:
- 140489
Reactions
Nitrite + acceptor = nitrate + reduced acceptor. |
- General function:
- Involved in nitrogen compound metabolic process
- Specific function:
- Plays a role in nitrite reduction
- Gene Name:
- nrfA
- Uniprot ID:
- P0ABK9
- Molecular weight:
- 53703
Reactions
NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+). |
- General function:
- Involved in nitrate reductase activity
- Specific function:
- This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit
- Gene Name:
- narV
- Uniprot ID:
- P0AF32
- Molecular weight:
- 26018
Reactions
Nitrite + acceptor = nitrate + reduced acceptor. |
- General function:
- Involved in iron-sulfur cluster binding
- Specific function:
- The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
- Gene Name:
- narH
- Uniprot ID:
- P11349
- Molecular weight:
- 58066
Reactions
Nitrite + acceptor = nitrate + reduced acceptor. |
- General function:
- Involved in nitrate reductase activity
- Specific function:
- The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit
- Gene Name:
- narI
- Uniprot ID:
- P11350
- Molecular weight:
- 25497
Reactions
Nitrite + acceptor = nitrate + reduced acceptor. |
- General function:
- Involved in unfolded protein binding
- Specific function:
- Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 2
- Gene Name:
- narW
- Uniprot ID:
- P19317
- Molecular weight:
- 26160
- General function:
- Involved in iron-sulfur cluster binding
- Specific function:
- This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit
- Gene Name:
- narY
- Uniprot ID:
- P19318
- Molecular weight:
- 58557
Reactions
Nitrite + acceptor = nitrate + reduced acceptor. |
- General function:
- Involved in oxidoreductase activity
- Specific function:
- The alpha chain is the actual site of nitrate reduction
- Gene Name:
- narZ
- Uniprot ID:
- P19319
- Molecular weight:
- 140226
Reactions
Nitrite + acceptor = nitrate + reduced acceptor. |
- General function:
- Involved in catalytic activity
- Specific function:
- (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+)
- Gene Name:
- lldD
- Uniprot ID:
- P33232
- Molecular weight:
- 42728
Reactions
(S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c + 2 H(+). |
- General function:
- Involved in oxidoreductase activity
- Specific function:
- Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein napC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism
- Gene Name:
- napA
- Uniprot ID:
- P33937
- Molecular weight:
- 93041
Reactions
Nitrite + acceptor = nitrate + reduced acceptor. |
- General function:
- Involved in electron carrier activity
- Specific function:
- 2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O
- Gene Name:
- yhjA
- Uniprot ID:
- P37197
- Molecular weight:
- 51570
Reactions
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O. |
- General function:
- Involved in unfolded protein binding
- Specific function:
- Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with the NarI subunit on the membrane
- Gene Name:
- narJ
- Uniprot ID:
- P0AF26
- Molecular weight:
- 26449
- General function:
- Not Available
- Specific function:
- Not Available
- Gene Name:
- nrfE
- Uniprot ID:
- P32710
- Molecular weight:
- Not Available