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Literature summary for 1.1.2.3 extracted from

  • Diep Le, K.H.; Lederer, F.; Golinelli-Pimpaneau, B.
    Structural evidence for the functional importance of the heme domain mobility in flavocytochrome b2 (2010), J. Mol. Biol., 400, 518-530.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, using 20% polyethylene glycol 4000, 0.1 M MES, pH 6.5, and 0.2 M MgCl2, at 18°C Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion mitochondrial intermembrane space Saccharomyces cerevisiae 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lactate + ferricytochrome c Saccharomyces cerevisiae
-
pyruvate + ferrocytochrome c + H+
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P00175
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lactate + ferricytochrome c
-
Saccharomyces cerevisiae pyruvate + ferrocytochrome c + H+
-
?

Subunits

Subunits Comment Organism
homotetramer x-ray crystallography Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Fcb2
-
Saccharomyces cerevisiae
flavocytochrome b2
-
Saccharomyces cerevisiae
L-lactate:cytochrome c oxidoreductase
-
Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
Saccharomyces cerevisiae
heme each enzyme subunit contains a cytochrome b5-like heme domain Saccharomyces cerevisiae