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Analysis of the domain properties of the novel cytochrome P450 RhF
Author(s) -
Hunter Dominic J.B.,
Roberts Gareth A.,
Ost Tobias W.B.,
White John H.,
Müller Steffen,
Turner Nicholas J.,
Flitsch Sabine L.,
Chapman Stephen K.
Publication year - 2005
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/j.febslet.2005.03.016
Subject(s) - flavin mononucleotide , chemistry , flavin group , ferredoxin , cofactor , stereochemistry , imidazole , enzyme , porphyrin , flavin adenine dinucleotide , heme , flavoprotein , photochemistry , biochemistry
The properties of the heme, flavin mononucleotide (FMN) and FeS domains of P450 RhF, from Rhodococcus sp. NCIMB 9784, expressed separately and in combination are analysed. The nucleotide preference, imidazole binding and reduction potentials of the heme and FMN domains are unaltered by their separation. The intact enzyme is monomeric and the flavin is confirmed to be FMN. The two one‐electron reduction potentials of the FMN are −240 and −270 mV. The spectroscopic and thermodynamic properties of the FeS domain, masked in the intact enzyme, are revealed for the first time, confirming it as a 2Fe–2S ferredoxin with a reduction potential of −214 mV.