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Investigating the effect of available redox protein ratios for the conversion of a steroid by a myxobacterial CYP 260A1
Author(s) -
Khatri Yogan,
Schifrin Alexander,
Bernhardt Rita
Publication year - 2017
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 - 10.1002/1873-3468.12619
Subject(s) - adrenodoxin , redox , monooxygenase , chemistry , biochemistry , substrate (aquarium) , cytochrome p450 , reductase , enzyme , combinatorial chemistry , stereochemistry , biophysics , biology , organic chemistry , ecology
Since cytochromes P450 are external monooxygenases, available surrogate redox partners have been used to reconstitute the P450 activity. However, the effect of various ratios of P450s and the redox proteins have not been extensively studied so far, although different combinations of the redox partners have shown variations in substrate conversion. To address this issue, CYP 260A1 was reconstituted with various ratios of adrenodoxin and adrenodoxin reductase to convert 11‐deoxycorticosterone, and the products were characterized by NMR . We show the effect of the available redox protein ratios not only on the P450 catalytic activity but also on the product pattern.