Analysis of the domain properties of the novel cytochrome P450RhF
Analysis of the domain properties of the novel cytochrome P450RhF
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DOI：
10.1016/j.febslet.2005.03.016
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发表时间：
2005-04-11
期刊：
影响因子：
3.5
通讯作者：
Chapman, SK
中科院分区：
文献类型：
--
作者：
Hunter, DJB;Roberts, GA;Chapman, SK
本文分析了红球菌NCIMB 9784 P450 RhF单独表达和联合表达的血红素、黄素单核苷酸（FMN）和FeS结构域的性质。血红素和FMN结构域的核苷酸偏好、咪唑结合和还原电位未因其分离而改变。完整酶为单体，黄素为FMN。FMN的两个单电子还原电位分别为-240和-270 mV。本文首次揭示了完整酶中FeS结构域的光谱和热力学性质，证实其为2Fe-2S铁氧还蛋白，还原电位为-214 mV。(c) 2005年由Elsevier B.V.代表欧洲生化学会联合会出版。
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.