Analysis of the domain properties of the novel cytochrome P450RhF

被引：47

作者：

Hunter, DJB ^{[1
]}

Roberts, GA ^{[1
]}

Ost, TWB ^{[1
]}

White, JH ^{[1
]}

Müller, S ^{[1
]}

Turner, NJ ^{[1
]}

Flitsch, SL ^{[1
]}

Chapman, SK ^{[1
]}

机构：

[1] Univ Edinburgh, Sch Chem, Edinburgh EH9 3JJ, Midlothian, Scotland

来源：

FEBS LETTERS | 2005年 / 579卷 / 10期

基金：

英国生物技术与生命科学研究理事会;

关键词：

cytochrome p450; flavin; monooxygenase; rhodococcus; 2Fe-2S; reduction potential;

D O I：

10.1016/j.febslet.2005.03.016

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：2215 / 2220

页数：6

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