The status of high-valent metal oxo complexes in the P450 cytochromes

Thomas M. Makris; Konstanze von Koenig; Ilme Schlichting; Stephen G. Sligar

doi:10.1016/j.jinorgbio.2006.01.025

The status of high-valent metal oxo complexes in the P450 cytochromes

Thomas M. Makris, Konstanze von Koenig, Ilme Schlichting, Stephen G. Sligar

Research output: Contribution to journal › Review article › peer-review

Abstract

The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.

Original language	English (US)
Pages (from-to)	507-518
Number of pages	12
Journal	Journal of Inorganic Biochemistry
Volume	100
Issue number	4
DOIs	https://doi.org/10.1016/j.jinorgbio.2006.01.025
State	Published - Apr 2006

Keywords

Compound I
Ferryl
Metal-Oxo
P450
X-ray

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

Online availability

10.1016/j.jinorgbio.2006.01.025

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title = "The status of high-valent metal oxo complexes in the P450 cytochromes",

abstract = "The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.",

keywords = "Compound I, Ferryl, Metal-Oxo, P450, X-ray",

author = "Makris, {Thomas M.} and Koenig, {Konstanze von} and Ilme Schlichting and Sligar, {Stephen G.}",

note = "Funding Information: This work was supported by a Merit Award the National Institutes of Health SGS) GM31756 and by the Deutsche Forschungsgemeinschaft (IS). We are grateful to Dr. Robert Gennis and Dan Han for the generous use of their stopped-flow instrument. ",

year = "2006",

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AU - Makris, Thomas M.

AU - Koenig, Konstanze von

AU - Schlichting, Ilme

AU - Sligar, Stephen G.

N1 - Funding Information: This work was supported by a Merit Award the National Institutes of Health SGS) GM31756 and by the Deutsche Forschungsgemeinschaft (IS). We are grateful to Dr. Robert Gennis and Dan Han for the generous use of their stopped-flow instrument.

PY - 2006/4

Y1 - 2006/4

N2 - The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.

AB - The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex, or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented.

KW - Compound I

KW - Ferryl

KW - Metal-Oxo

KW - P450

KW - X-ray

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DO - 10.1016/j.jinorgbio.2006.01.025

M3 - Review article

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SN - 0162-0134

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JO - Journal of Inorganic Biochemistry

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The status of high-valent metal oxo complexes in the P450 cytochromes

Abstract

Keywords

ASJC Scopus subject areas

Online availability

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