title: Analysis of the domain properties of the novel cytochrome P450 RhF.
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.
authors.affiliation: School of Chemistry, University of Edinburgh, The King's Buildings, West Mains Road, Edinburgh EH9 3JJ, UK.
authors.forename: Dominic J B
authors.initials: DJ
authors.lastname: Hunter
authors.forename: Gareth A
authors.initials: GA
authors.lastname: Roberts
authors.forename: Tobias W B
authors.initials: TW
authors.lastname: Ost
authors.forename: John H
authors.initials: JH
authors.lastname: White
authors.forename: Steffen
authors.initials: S
authors.lastname: Müller
authors.forename: Nicholas J
authors.initials: NJ
authors.lastname: Turner
authors.forename: Sabine L
authors.initials: SL
authors.lastname: Flitsch
authors.forename: Stephen K
authors.initials: SK
authors.lastname: Chapman
mesh_terms: D001483:Base Sequence; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D017931:DNA Primers; D004578:Electron Spin Resonance Spectroscopy; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism*; D012240:Rhodococcus / Q000201:enzymology*; D013816:Thermodynamics
chemical_list: D017931:DNA Primers; D007527:Isoenzymes; D003577:Cytochrome P-450 Enzyme System