Analysis of the domain properties of the novel cytochrome P450RhF

Dominic J B Hunter, Gareth A Roberts, Tobias W B Ost, John H White, Steffen Müller, Nicholas J Turner, Sabine L Flitsch, Stephen K Chapman

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    Abstract

    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.

    Original languageEnglish
    Pages (from-to)2215-2220
    Number of pages6
    JournalFEBS Letters
    Volume579
    Issue number10
    DOIs
    Publication statusPublished - 11 Apr 2005

    Keywords

    • reduction potential
    • monooxygenase
    • 2Fe-2S
    • PHTHALATE DIOXYGENASE REDUCTASE
    • cytochrome p450
    • GENE-CLUSTER
    • DEGRADATION
    • flavin
    • SELF-SUFFICIENT CYTOCHROME-P450
    • rhodococcus
    • BACILLUS-MEGATERIUM
    • RHODOCOCCUS SP

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