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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

Summary:
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 [Gray82, 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: periplasmic space

Molecular Weight: 57 kD (experimental)

Gene-Reaction Schematic: ?

GO Terms:

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

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


Enzymatic reaction of: flavocytochrome c sulfide dehydrogenase

EC Number: 1.8.2.3

hydrogen sulfide + 2 an oxidized c-type cytochrome <=> S0 + 2 a reduced c-type cytochrome + 2 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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:IPR015904 , 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


References

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

Chen94c: 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

Gray82: 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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, BIOCYC14A.