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MetaCyc Protein Class: an oxidized c-type cytochrome

Synonyms: a ferri c-type cytochrome

Superclasses: a cytochromea c-type cytochrome
a cytochromean oxidized cytochrome

Summary:
C-type cytochromes (cytC) are electron-transfer proteins that have one or more heme c groups that are bound to the protein by one or two thioether bonds involving sulfhydryl groups of cysteine residues. C-type cytochromes possess a wide range of properties and function in a large number of different redox processes. In general, the differences in c-type cytochromes among bacteria are much larger than those among animal species. The use of the term term "c-type cytochromes" was introduced to distinguish this family of diverse proteins from the well-characterized mitochondrial protein, which is often referred to as "cytochrome c".

Bacterial c-type cytochromes function in the electron transport chains of bacteria with many different types of energy metabolism, including phototrophs, methylotrophs, denitrifiers, sulfate reducers and the nitrogen-fixers.

The C-type cytochromes have been classified in four classes based on their sequence (reviewed in [Ambler91]):

Class I includes the low-spin soluble cytC of mitochondria and bacteria, with the heme-attachment site towards the N-terminus, and the sixth ligand provided by a methionine residue about 40 residues further on towards the C-terminus. Memebers of this class were further subdivided into the five subclasses, IA to IE, which are named long cytochrome c2, mitochondrial cytochrome c, split-a-band cytochromes c, cytochrome c8 and cytochrome c5, respectively .

Class II includes the high-spin cytochromes c' and various low-spin cytochromes (e.g., Rhodopseudomonas palustris cytochrome c-556). The heme-attachment site is close to the C-terminus and in the low-spin proteins the sixth ligand is a methionine residue close to the N-terminus.

Class III comprises the low redox potential multiple heme cytochromes c3 and c7, with only around thirty residues of amino acid per heme group.

Class IV was created to hold the complex proteins that have other prosthetic groups as well as heme c, such as the flavocytochromes c and the cytochromes cd.

an oxidized <i>c</i>-type cytochrome compound structure

Child Classes: an oxidized cytochrome c-553 (0), an oxidized cytochrome c2 (0), an oxidized cytochrome c3 (0), an oxidized cytochrome c4 (0), an oxidized cytochrome c550 (0), an oxidized cytochrome c551 (0), an oxidized cytochrome c552 (1), an oxidized cytochrome c554 (0), an oxidized cytochrome cL (0), an oxidized cytochrome cm552 (0)

Instances:
formate-dependent nitrite reductase - penta-heme cytochrome c (Escherichia coli K-12 substr. MG1655) ,
SoxE (Paracoccus pantotrophus)

SMILES: CC2(=C(CCC(=O)[O-])C8(=[N+]3([Fe-]46([N+]1(=C(C(C(C)S[a c-type cytochrome])=C(C)C1=CC5(=C(C(C)S[a c-type cytochrome])C(C)=C(C=C23)N45))C=C7(C(C)=C(CCC(=O)[O-])C(N67)=C8))))))

Unification Links: KEGG:C00125

Reactions known to consume the compound:

ammonia oxidation I (aerobic) :
4 an oxidized c-type cytochrome[out] + hydroxylamine[in] + H2O[in] → 4 a reduced c-type cytochrome[out] + nitrite[in] + 5 H+[in]

ammonia oxidation IV (autotrophic ammonia oxidizers) :
4 an oxidized c-type cytochrome[out] + hydroxylamine[in] + H2O[in] → 4 a reduced c-type cytochrome[out] + nitrite[in] + 5 H+[in]
a reduced cytochrome c554 + an oxidized c-type cytochrome → an oxidized cytochrome c554 + a reduced c-type cytochrome

arsenite oxidation I (respiratory) :
2 a reduced c-type cytochrome[periplasm] + arsenate + 3 H+ ← 2 an oxidized c-type cytochrome[periplasm] + arsenite + H2O

L-ascorbate biosynthesis I (L-galactose pathway) :
L-galactono-1,4-lactone + 2 an oxidized c-type cytochrome → L-ascorbate + 2 a reduced c-type cytochrome + 3 H+

L-ascorbate biosynthesis II (L-gulose pathway) :
L-gulono-1,4-lactone + 2 an oxidized c-type cytochrome → L-ascorbate + 2 a reduced c-type cytochrome + 3 H+

methylglyoxal degradation V :
(S)-lactate + 2 an oxidized c-type cytochrome → pyruvate + 2 a reduced c-type cytochrome + 2 H+

methylglyoxal degradation VI :
(R)-lactate + 2 an oxidized c-type cytochrome → pyruvate + 2 a reduced c-type cytochrome + 2 H+

nitrifier denitrification :
hydroxylamine + 3 an oxidized c-type cytochrome → nitric oxide + 3 a reduced c-type cytochrome + 3 H+

nitrite oxidation :
2 an oxidized c-type cytochrome[out] + nitrite[in] + H2O[in] → 2 a reduced c-type cytochrome[out] + nitrate[in] + 2 H+[in]

polyvinyl alcohol degradation :
polyvinyl alcohol(n) + 2n an oxidized c-type cytochrome → oxidized polyvinyl alcohol(n) + 2n a reduced c-type cytochrome + 2n H+

sulfide oxidation II (sulfide dehydrogenase) :
hydrogen sulfide + 2 an oxidized c-type cytochrome → S0 + 2 a reduced c-type cytochrome + 2 H+

sulfite oxidation I (sulfite oxidoreductase) :
sulfite + 2 an oxidized c-type cytochrome + H2O → sulfate + 2 a reduced c-type cytochrome + 2 H+

thiosulfate oxidation I (to tetrathionate) :
2 an oxidized c-type cytochrome[periplasm] + 2 thiosulfate[periplasm] → tetrathionate[periplasm] + 2 a reduced c-type cytochrome[periplasm] + 2 H+[periplasm]

thiosulfate oxidation III (multienzyme complex) :
a [SoxY protein]-S-thiocysteine + 6 an oxidized c-type cytochrome + 3 H2O → a [SoxY protein]-L-cysteine-S-sulfate + 6 a reduced c-type cytochrome + 7 H+
a [SoxY protein]-L-cysteine + thiosulfate + 2 an oxidized c-type cytochrome → a [SoxY protein]-thiocysteine-S-sulfate + 2 a reduced c-type cytochrome + 2 H+

thiosulfate oxidation IV (multienzyme complex) :
a [SoxY protein]-L-cysteine + thiosulfate + 2 an oxidized c-type cytochrome → a [SoxY protein]-thiocysteine-S-sulfate + 2 a reduced c-type cytochrome + 2 H+

Not in pathways:
2 an oxidized c-type cytochrome[out] + a menaquinol[membrane] → 2 a reduced c-type cytochrome[out] + a menaquinone[membrane] + 2 H+[in]
2 an oxidized c-type cytochrome[out] + an electron-transfer quinol[membrane] → 2 a reduced c-type cytochrome[out] + an electron-transfer quinone[membrane] + 2 H+[in]
L-ascorbate + 2 an oxidized c-type cytochrome → L-dehydro-ascorbate + 2 a reduced c-type cytochrome + H+

nicotinate degradation I :
nicotinate + 2 an oxidized cytochrome + H2O → 6-hydroxynicotinate + 2 a reduced cytochrome + 2 H+

Reactions known to produce the compound:

aerobic respiration I (cytochrome c) , aerobic respiration II (cytochrome c) (yeast) , arsenite oxidation I (respiratory) :
4 a reduced c-type cytochrome[out] + oxygen[in] + 8 H+[in] → 4 an oxidized c-type cytochrome[out] + 4 H+[out] + 2 H2O[in]

ammonia oxidation II (anaerobic) , nitrite-dependent anaerobic methane oxidation :
nitric oxide + an oxidized c-type cytochrome + H2O ← nitrite + a reduced c-type cytochrome + 2 H+

Fe(II) oxidation :
4 a reduced c-type cytochrome[periplasm] + oxygen + 8 H+ → 4 an oxidized c-type cytochrome[periplasm] + 4 H+[periplasm] + 2 H2O

nitrate reduction I (denitrification) :
2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] → 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]

nitrate reduction IV (dissimilatory) :
nitrite[out] + 6 a reduced c-type cytochrome[out] + 8 H+[out] → ammonium[out] + 6 an oxidized c-type cytochrome[out] + 2 H2O[out]
nitrate[periplasm] + 2 a reduced c-type cytochrome[periplasm] + 2 H+[periplasm] → nitrite[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]

nitrate reduction VII (denitrification) :
2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] → 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
nitric oxide + an oxidized c-type cytochrome + H2O ← nitrite + a reduced c-type cytochrome + 2 H+

nitrifier denitrification :
2 a reduced c-type cytochrome[periplasm] + nitrous oxide[periplasm] + 2 H+[periplasm] → 2 an oxidized c-type cytochrome[periplasm] + N2[periplasm] + H2O[periplasm]
nitric oxide + an oxidized c-type cytochrome + H2O ← nitrite + a reduced c-type cytochrome + 2 H+

Not in pathways:
nitroxyl + 2 a reduced c-type cytochrome + oxygen + H+ → nitrite + 2 an oxidized c-type cytochrome + H2O

Reactions known to both consume and produce the compound:

aerobic respiration I (cytochrome c) , aerobic respiration II (cytochrome c) (yeast) , ammonia oxidation IV (autotrophic ammonia oxidizers) :
2 an oxidized c-type cytochrome[out] + an ubiquinol[membrane] ↔ 2 a reduced c-type cytochrome[out] + a ubiquinone[membrane] + 2 H+[out]

nitrate reduction I (denitrification) , nitrifier denitrification :
2 nitric oxide[periplasm] + 2 a reduced c-type cytochrome[periplasm] + 2 H+[periplasm] ↔ nitrous oxide[periplasm] + 2 an oxidized c-type cytochrome[periplasm] + H2O[periplasm]

Not in pathways:
a c-type cytochrome ↔ heme c + an apo-[c-type cytochrome]

In Reactions of unknown directionality:

Not in pathways:
Fe3+ + a reduced c-type cytochrome = Fe2+ + an oxidized c-type cytochrome
hydrogen peroxide + 2 a reduced c-type cytochrome + 2 H+ = 2 an oxidized c-type cytochrome + 2 H2O
glycine + 2 an oxidized c-type cytochrome + H2O = glyoxylate + ammonium + 2 a reduced c-type cytochrome + 2 H+
D-mannitol + 2 an oxidized c-type cytochrome = keto-D-fructose + 2 a reduced c-type cytochrome + 2 H+
hydroxylamine + 2 an oxidized c-type cytochrome = nitroxyl + 2 a reduced c-type cytochrome + 2 H+
trimethylamine + 2 an oxidized c-type cytochrome + H2O = trimethylamine N-oxide + 2 a reduced c-type cytochrome + 3 H+
ethanol + 2 an oxidized c-type cytochrome = acetaldehyde + 2 a reduced c-type cytochrome + 2 H+
L-gulono-1,4-lactone + 4 an oxidized c-type cytochrome = L-dehydro-ascorbate + 4 a reduced c-type cytochrome + 4 H+
lupanine + 2 an oxidized c-type cytochrome + H2O = 17-hydroxylupanine + 2 a reduced c-type cytochrome + 2 H+
L-galactono-1,4-lactone + 4 an oxidized c-type cytochrome = L-dehydro-ascorbate + 4 a reduced c-type cytochrome + 4 H+

In Redox half-reactions:
an oxidized c-type cytochrome[in] + e-[membrane] → a reduced c-type cytochrome[in],
an oxidized c-type cytochrome[out] + e-[membrane] → a reduced c-type cytochrome[out]

Enzymes inhibited by an oxidized c-type cytochrome, sorted by the type of inhibition, are:

Inhibitor (Mechanism unknown) of: autumnaline cytochrome P-450 oxidase [Nasreen96], O-methylandrocymbine cytochrome P450 oxidase [Rueffer98]

This compound has been characterized as a cofactor or prosthetic group of the following enzymes: nicotinate dehydrogenase, alcohol dehydrogenase, nitrate reductase

Gene-Reaction Schematic

Gene-Reaction Schematic

Credits:
Revised 18-Jan-2011 by Caspi R, SRI International


References

Ambler91: Ambler RP (1991). "Sequence variability in bacterial cytochromes c." Biochim Biophys Acta 1058(1);42-7. PMID: 1646017

Anderson88c: Anderson DJ, Lidstrom ME (1988). "The moxFG region encodes four polypeptides in the methanol-oxidizing bacterium Methylobacterium sp. strain AM1." J Bacteriol 170(5);2254-62. PMID: 3129405

Barker99: Barker PD, Ferguson SJ (1999). "Still a puzzle: why is haem covalently attached in c-type cytochromes?." Structure 7(12);R281-90. PMID: 10647174

BeardmoreGray82: Beardmore-Gray M, O'Keeffe DT, Anthony C (1982). "The autoreducible cytochromes c of the methylotrophs Methylophilus methylotrophus and Pseudomonas AM1." Biochem J 207(1);161-5. PMID: 6295363

Cavazza96: Cavazza C, Giudici-Orticoni MT, Nitschke W, Appia C, Bonnefoy V, Bruschi M (1996). "Characterisation of a soluble cytochrome c4 isolated from Thiobacillus ferrooxidans." Eur J Biochem 242(2);308-14. PMID: 8973648

Ceruso03: Ceruso MA, Grottesi A, Di Nola A (2003). "Dynamic effects of mutations within two loops of cytochrome c551 from Pseudomonas aeruginosa." Proteins 50(2);222-9. PMID: 12486716

Cutruzzola02: Cutruzzola F, Arese M, Ranghino G, van Pouderoyen G, Canters G, Brunori M (2002). "Pseudomonas aeruginosa cytochrome C(551): probing the role of the hydrophobic patch in electron transfer." J Inorg Biochem 88(3-4);353-61. PMID: 11897350

Darwin93: Darwin A, Tormay P, Page L, Griffiths L, Cole J (1993). "Identification of the formate dehydrogenases and genetic determinants of formate-dependent nitrite reduction by Escherichia coli K12." J Gen Microbiol 1993;139 ( Pt 8);1829-40. PMID: 8409924

Darwin93a: Darwin A, Hussain H, Griffiths L, Grove J, Sambongi Y, Busby S, Cole J (1993). "Regulation and sequence of the structural gene for cytochrome c552 from Escherichia coli: not a hexahaem but a 50 kDa tetrahaem nitrite reductase." Mol Microbiol 1993;9(6);1255-65. PMID: 7934939

Eaves98: Eaves DJ, Grove J, Staudenmann W, James P, Poole RK, White SA, Griffiths I, Cole JA (1998). "Involvement of products of the nrfEFG genes in the covalent attachment of haem c to a novel cysteine-lysine motif in the cytochrome c552 nitrite reductase from Escherichia coli." Mol Microbiol 28(1);205-16. PMID: 9593308

Fujita66: Fujita T (1966). "Studies on soluble cytochromes in Enterobacteriaceae. I. Detection, purification, and properties of cytochrome c-552 in anaerobically grown cells." J Biochem (Tokyo) 1966;60(2);204-15. PMID: 5338848

Gray96: Gray HB, Winkler JR (1996). "Electron transfer in proteins." Annu Rev Biochem 65;537-61. PMID: 8811189

Hussain94: Hussain H, Grove J, Griffiths L, Busby S, Cole J (1994). "A seven-gene operon essential for formate-dependent nitrite reduction to ammonia by enteric bacteria." Mol Microbiol 1994;12(1);153-63. PMID: 8057835

IobbiNivol94: Iobbi-Nivol C, Crooke H, Griffiths L, Grove J, Hussain H, Pommier J, Mejean V, Cole JA (1994). "A reassessment of the range of c-type cytochromes synthesized by Escherichia coli K-12." FEMS Microbiol Lett 1994;119(1-2);89-94. PMID: 8039676

Kadziola97: Kadziola A, Larsen S (1997). "Crystal structure of the dihaem cytochrome c4 from Pseudomonas stutzeri determined at 2.2A resolution." Structure 5(2);203-16. PMID: 9032080

Kodama69: Kodama T, Shidara S (1969). "Components of cytochrome system and purification and some properties of c-type cytochromes of a denitrifying bacterium, Pseudomonas stutzeri." J Biochem 65(3);351-60. PMID: 5789183

Matsuura82: Matsuura Y, Takano T, Dickerson RE (1982). "Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 A resolution and comparison of the two redox forms." J Mol Biol 156(2);389-409. PMID: 6283101

Munn86: Munn C A M (1886). "Researches on Myohaematin and the Histohaematins." Philosophical Transactions of the Royal Society of London 177(0);267-298.

Nasreen96: Nasreen, A., Rueffer, M, Zenk, M.H (1996). "Cytochrome P-450-dependent fromation of isoandrocymbine from autumnaline in colchicine biosynthesis." tetrahedron Letters, 37, 8161-8164.

Neumann59: Neumann NP, Burris RH (1959). "Cytochromes c4 and c5 of Azotobacter vinelandii: chromatographic purification, crystallization, and a study of their physical properties." J Biol Chem 234;3286-90. PMID: 14426712

Nunn88: Nunn DN, Anthony C (1988). "The nucleotide sequence and deduced amino acid sequence of the cytochrome cL gene of Methylobacterium extorquens AM1, a novel class of c-type cytochrome." Biochem J 256(2);673-6. PMID: 2851998

Nunn88a: Nunn DN, Anthony C (1988). "The nucleotide sequence and deduced amino acid sequence of the genes for cytochrome cL and a hypothetical second subunit of the methanol dehydrogenase of Methylobacterium AM1." Nucleic Acids Res 16(15);7722. PMID: 2842733

OKeeffe80: O'Keeffe DT, Anthony C (1980). "The two cytochromes c in the facultative methylotroph Pseudomonas am1." Biochem J 192(2);411-9. PMID: 6263253

Pope84: Pope NR, Cole JA (1984). "Pyruvate and ethanol as electron donors for nitrite reduction by Escherichia coli K12." J Gen Microbiol 1984;130 ( Pt 5);1279-84. PMID: 6381645

Rueffer98: Rueffer, M, Zenk, M.H (1998). "Microsome-mediated transformation of O-methylandrocymbine to demecolcine and colchicine." FEBS letters, 438, 111-113.

Sawyer81: Sawyer L, Jones CL, Damas AM, Harding MM, Gould RO, Ambler RP (1981). "Cytochrome c4 from Pseudomonas aeruginosa." J Mol Biol 153(3);831-5. PMID: 6279879

Schobert99: Schobert M, Gorisch H (1999). "Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase." Microbiology 145 ( Pt 2);471-81. PMID: 10075429

Timkovich98: Timkovich R, Bergmann D, Arciero DM, Hooper AB (1998). "Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea." Biophys J 75(4);1964-72. PMID: 9746537

Van91a: Van Spanning RJ, Wansell CW, De Boer T, Hazelaar MJ, Anazawa H, Harms N, Oltmann LF, Stouthamer AH (1991). "Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growth." J Bacteriol 173(21);6948-61. PMID: 1657871


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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