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Literature summary for 1.6.2.4 extracted from

  • Lamb, D.C.; Kim, Y.; Yermalitskaya, L.V.; Yermalitsky, V.N.; Lepesheva, G.I.; Kelly, S.L.; Waterman, M.R.; Podust, L.M.
    A second FMN binding site in yeast NADPH-cytochrome P450 reductase suggests a mechanism of electron transfer by diflavin reductases (2006), Structure, 14, 51-61.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of truncated yeast NADPH-cytochrome P450 reductase, which is functionally active toward its physiological substrate cytochrome P450 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P16603
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricytochrome c + NADPH
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Saccharomyces cerevisiae 2 ferrocytochrome c + NADP+ + H+
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?

Synonyms

Synonyms Comment Organism
NADPH-cytochrome P450 reductase
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FMN second FMN binding site is detected at the interface of the connecting and FMN binding domains. The two FMN binding sites have different accessibilities to the bulk solvent and different amino acid environments, suggesting stabilization of different electronic structures of the reduced flavin. Since only one FMN cofactor is required for function, a hypothetical mechanism of electron transfer is discussed that proposes shuttling of a single FMN between these two sites coupled with the transition between two semiquinone forms, neutral and anionic Saccharomyces cerevisiae