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 [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)
|Cellular Component:||GO:0030288 - outer membrane-bounded periplasmic space [Dolata93]|
Enzymatic reaction of: flavocytochrome c sulfide dehydrogenase
EC Number: 188.8.131.52
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)
|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: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
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
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