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Structural and enzymological analysis of the interaction of isolated domains of cytochrome P ‐450 BM3
Author(s) -
Munro Andrew W.,
Lindsay J.Gordon,
Coggins John R.,
Kelly Sharon M.,
Price Nicholas C.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80609-8
Subject(s) - flavin group , cytochrome , chemistry , cytochrome c , electron transfer , flavin adenine dinucleotide , biochemistry , flavin mononucleotide , stereochemistry , cofactor , enzyme , photochemistry , mitochondrion
The interactions of the individually expressed haem‐ and flavin‐containing domains of cytochrome P ‐450 BM3 have been analysed by enzymological and spectroscopic techniques. Electron transfer between the isolated domains occurs at a much lower rate than that occurring in the intact flavocytochrome. CD spectroscopic studies indicate that the linkage of the domains in intact P ‐450 BM3 creates haem and amino acid environments suitable for efficient electron transfer from its flavin domain.