Species: Allochromatium vinosum
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 [Gray82a, 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.
Molecular Weight: 57 kD (experimental)
Enzymatic reaction of: flavocytochrome c sulfide dehydrogenase
EC Number: 188.8.131.52hydrogen 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)
|Gene:||fccA||Accession Number: G-9509 (MetaCyc)|
Molecular Weight: 21.636 kD (from nucleotide sequence)
Molecular Weight: 21 kD (experimental) [Fukumori79]
|Gene:||fccB||Accession Number: G-9510 (MetaCyc)|
Molecular Weight: 45.898 kD (from nucleotide sequence)
Molecular Weight: 46 kD (experimental) [Fukumori79]
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
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
Chen94a: 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
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
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
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493