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MetaCyc Enzyme: flavocytochrome c sulfide dehydrogenase

Species: Allochromatium vinosum

Subunit composition of flavocytochrome c sulfide dehydrogenase = [FccA][FccB]
         flavocytochrome c cytochrome subunit = FccA
         flavocytochrome c flavoprotein subunit = FccB

The flavocytochrome c sulfide dehydrogenase of Allochromatium vinosum was first isolated in 1960, long before it was known that the enzyme oxidizes sulfide [Bartsch60]. The true activity of the enzyme was discovered much later [Kusai73]. The enzyme is a heterodimer, composed of a cytochrome c552 subunit and a flavoprotein subunit [Fukumori79, Yamanaka79]. The enzyme has been characterized extensively [Gray82c, Bosshard86, Vieira86]. The cytochrome subunit contains two heme molecules [Van91], and sequence information confirmed that the enzyme is periplasmic [Dolata93].

Somewhat surprisingly, disruption of the genes encoding the enzyme in Allochromatium vinosum did not have any significant effect on the sulfide oxidizing abillity of this organism [Reinartz98]. It has been suggested that in this organism the enzyme may be involved in a high affinity sulfide oxidation system, which functions only only under conditions of very low sulfide concentrations.

Locations: periplasm

Molecular Weight: 57 kD (experimental)

Gene-Reaction Schematic

Gene-Reaction Schematic

GO Terms:
Cellular Component:
GO:0030288 - outer membrane-bounded periplasmic space [Dolata93]

Created 03-Aug-2006 by Caspi R, SRI International

Enzymatic reaction of: flavocytochrome c sulfide dehydrogenase

Inferred from experiment

EC Number:

hydrogen sulfide + 2 an oxidized c-type cytochrome → S0 + 2 a reduced c-type cytochrome + 2 H+

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: sulfide oxidation II (sulfide dehydrogenase)

Subunit of flavocytochrome c sulfide dehydrogenase: flavocytochrome c cytochrome subunit

Synonyms: FccA

Gene: fccA Accession Number: G-9509 (MetaCyc)

Molecular Weight: 21.636 kD (from nucleotide sequence)

Molecular Weight: 21 kD (experimental) [Fukumori79]

Unification Links: DIP:DIP-6170N, Protein Model Portal:Q06529, SMR:Q06529, UniProt:Q06529

Relationship Links: InterPro:IN-FAMILY:IPR009056, InterPro:IN-FAMILY:IPR024167, PDB:Structure:1FCD, Prosite:IN-FAMILY:PS51007

Subunit of flavocytochrome c sulfide dehydrogenase: flavocytochrome c flavoprotein subunit

Synonyms: FccB

Gene: fccB Accession Number: G-9510 (MetaCyc)

Molecular Weight: 45.898 kD (from nucleotide sequence)

Molecular Weight: 46 kD (experimental) [Fukumori79]

Unification Links: DIP:DIP-6169N, Protein Model Portal:Q06530, SMR:Q06530, UniProt:Q06530

Relationship Links: InterPro:IN-FAMILY:IPR006311, InterPro:IN-FAMILY:IPR015323, InterPro:IN-FAMILY:IPR016156, InterPro:IN-FAMILY:IPR019546, InterPro:IN-FAMILY:IPR023753, Panther:IN-FAMILY:PTHR10632, PDB:Structure:1FCD, Pfam:IN-FAMILY:PF07992, Pfam:IN-FAMILY:PF09242, Prosite:IN-FAMILY:PS51318


Bartsch60: Bartsch RG, Kamen MD (1960). "Isolation and properties of two soluble heme proteins in extracts of the photoanaerobe Chromatium." J Biol Chem 235;825-31. PMID: 13797318

Bosshard86: Bosshard HR, Davidson MW, Knaff DB, Millett F (1986). "Complex formation and electron transfer between mitochondrial cytochrome c and flavocytochrome c552 from Chromatium vinosum." J Biol Chem 261(1);190-3. PMID: 3001047

Chen94b: Chen ZW, Koh M, Van Driessche G, Van Beeumen JJ, Bartsch RG, Meyer TE, Cusanovich MA, Mathews FS (1994). "The structure of flavocytochrome c sulfide dehydrogenase from a purple phototrophic bacterium." Science 266(5184);430-2. PMID: 7939681

Dolata93: Dolata MM, Van Beeumen JJ, Ambler RP, Meyer TE, Cusanovich MA (1993). "Nucleotide sequence of the heme subunit of flavocytochrome c from the purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA fragment contains two multiheme cytochromes, a flavoprotein, and a homolog of human ankyrin." J Biol Chem 268(19);14426-31. PMID: 8390993

Fukumori79: Fukumori Y, Yamanaka T (1979). "Flavocytochrome c of Chromatium vinosum. Some enzymatic properties and subunit structure." J Biochem (Tokyo) 85(6);1405-14. PMID: 222744

Gray82c: Gray, G. O., Knaff, D. B. (1982). "Role of a cytochrome c-552 - cytochrome c complex in the oxidation of sulfide in Chromatium vinosum." Biochim. Biophys. Acta, 680: 290-296.

Kusai73: Kusai K, Yamanaka T (1973). "The oxidation mechanisms of thiosulphate and sulphide in Chlorobium thiosulphatophilum: roles of cytochrome c-551 and cytochrome c-553." Biochim Biophys Acta 325(2);304-14. PMID: 4357558

Reinartz98: Reinartz M, Tschape J, Bruser T, Truper HG, Dahl C (1998). "Sulfide oxidation in the phototrophic sulfur bacterium Chromatium vinosum." Arch Microbiol 170(1);59-68. PMID: 9639604

Van91: Van Beeumen JJ, Demol H, Samyn B, Bartsch RG, Meyer TE, Dolata MM, Cusanovich MA (1991). "Covalent structure of the diheme cytochrome subunit and amino-terminal sequence of the flavoprotein subunit of flavocytochrome c from Chromatium vinosum." J Biol Chem 266(20);12921-31. PMID: 1649169

Vieira86: Vieira B, Davidson M, Knaff D, Millett F (1986). "The use of a water-soluble carbodiimide to study the interaction between Chromatium vinosum flavocytochrome c-552 and cytochrome c." Biochim Biophys Acta 848(1);131-6. PMID: 3002455

Yamanaka79: Yamanaka T, Fukumori Y, Okunuki K (1979). "Preparation of subunits of flavocytochromes c derived from Chlorobium limicola f. thiosulfatophilum and Chromatium vinosum." Anal Biochem 95(1);209-13. PMID: 227287

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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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