Member database | CDD |
CDD type | domain |
Short name | FCB2_FMN |
Set | TIM |
Description
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.
[3, 4, 2, 1, 5]References
1.Flavocytochromes: structures and implications for electron transfer. Cunane LM, Chen ZW, Durley RC, Barton JD, Mathews FS. Biochem Soc Trans 27, 179-84, (1999). PMID: 10093730
3.Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme. Cunane LM, Barton JD, Chen ZW, Welsh FE, Chapman SK, Reid GA, Mathews FS. Biochemistry 41, 4264-72, (2002). View articlePMID: 11914072
4.Altered substrate specificity in flavocytochrome b2: structural insights into the mechanism of L-lactate dehydrogenation. Mowat CG, Wehenkel A, Green AJ, Walkinshaw MD, Reid GA, Chapman SK. Biochemistry 43, 9519-26, (2004). View articlePMID: 15260495