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

doi:10.1016/j.febslet.2005.03.016

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

Research output: Contribution to journal › Article › peer-review

52 Citations (Scopus)

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 language	English
Pages (from-to)	2215-2220
Number of pages	6
Journal	FEBS Letters
Volume	579
Issue number	10
DOIs	https://doi.org/10.1016/j.febslet.2005.03.016
Publication status	Published - 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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10.1016/j.febslet.2005.03.016

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title = "Analysis of the domain properties of the novel cytochrome P450RhF",

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.",

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

author = "Hunter, {Dominic J B} and Roberts, {Gareth A} and Ost, {Tobias W B} and White, {John H} and Steffen M{\"u}ller and Turner, {Nicholas J} and Flitsch, {Sabine L} and Chapman, {Stephen K}",

year = "2005",

month = apr,

day = "11",

doi = "10.1016/j.febslet.2005.03.016",

language = "English",

volume = "579",

pages = "2215--2220",

journal = "FEBS Letters",

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TY - JOUR

T1 - Analysis of the domain properties of the novel cytochrome P450RhF

AU - Hunter, Dominic J B

AU - Roberts, Gareth A

AU - Ost, Tobias W B

AU - White, John H

AU - Müller, Steffen

AU - Turner, Nicholas J

AU - Flitsch, Sabine L

AU - Chapman, Stephen K

PY - 2005/4/11

Y1 - 2005/4/11

N2 - 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.

AB - 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.

KW - reduction potential

KW - monooxygenase

KW - 2Fe-2S

KW - PHTHALATE DIOXYGENASE REDUCTASE

KW - cytochrome p450

KW - GENE-CLUSTER

KW - DEGRADATION

KW - flavin

KW - SELF-SUFFICIENT CYTOCHROME-P450

KW - rhodococcus

KW - BACILLUS-MEGATERIUM

KW - RHODOCOCCUS SP

U2 - 10.1016/j.febslet.2005.03.016

DO - 10.1016/j.febslet.2005.03.016

M3 - Article

SN - 0014-5793

VL - 579

SP - 2215

EP - 2220

JO - FEBS Letters

JF - FEBS Letters

IS - 10

ER -

Analysis of the domain properties of the novel cytochrome P450RhF

Abstract

Keywords

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