Analysis of the domain properties of the novel cytochrome P450 RhF
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 separat...
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Published in | FEBS letters Vol. 579; no. 10; pp. 2215 - 2220 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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England
Elsevier B.V
11.04.2005
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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. |
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AbstractList | 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. 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. 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. 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. 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 -270mV. 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 -214mV. |
Author | Roberts, Gareth A. Hunter, Dominic J.B. White, John H. Müller, Steffen Ost, Tobias W.B. Turner, Nicholas J. Flitsch, Sabine L. Chapman, Stephen K. |
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Copyright | 2005 FEBS Letters 579 (2005) 1873-3468 © 2015 Federation of European Biochemical Societies |
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Keywords | FMN Cytochrome P450 FAD OTTLE Rhodococcus Reduction potential PPM Monooxygenase HPLC–MS 2Fe–2S SHE Flavin PMSF LB ALA IPTG NAD(P)H |
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Snippet | The properties of the heme, flavin mononucleotide (FMN) and FeS domains of P450 RhF, from
Rhodococcus sp. NCIMB 9784, expressed separately and in combination... The properties of the heme, flavin mononucleotide (FMN) and FeS domains of P450 RhF, from Rhodococcus sp. NCIMB 9784, expressed separately and in combination... The properties of the heme, flavin mononucleotide (FMN) and FeS domains of P450 RhF, from Rhodococcus sp. NCIMB 9784, expressed separately and in combination... |
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SubjectTerms | 2Fe–2S 5-amino-4-oxo-pentanoic acid ALA Base Sequence Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 DNA Primers Electron Spin Resonance Spectroscopy FAD Flavin flavin adenine dinucleotide flavin mononucleotide FMN high performance liquid chromatography–mass spectrometry HPLC–MS IPTG Isoenzymes - chemistry Isoenzymes - metabolism isopropyl β-d-1-thiogalactopyranoside Luria–Bertani medium Monooxygenase NAD(P)H nicotinamide adenine dinucleotide (phosphate), reduced form optically transparent thin layer electrochemistry OTTLE parts per million phenylmethylsulfonyl fluoride PMSF PPM Reduction potential Rhodococcus Rhodococcus - enzymology SHE standard hydrogen electrode Thermodynamics |
Title | Analysis of the domain properties of the novel cytochrome P450 RhF |
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