Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies

Roman Davydov; Brian M. Hoffman

doi:10.1016/j.abb.2010.09.013

Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies

Roman Davydov, Brian M. Hoffman

Chemistry

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

54 Scopus citations

Abstract

This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.

Original language	English (US)
Pages (from-to)	36-43
Number of pages	8
Journal	Archives of biochemistry and biophysics
Volume	507
Issue number	1
DOIs	https://doi.org/10.1016/j.abb.2010.09.013
State	Published - Mar 1 2011

Keywords

Cryoreduction
Cytochrome P450
Dioxygen activation
ENDOR
EPR
Heme oxygenase
Nitric oxide synthase

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry

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10.1016/j.abb.2010.09.013

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title = "Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies",

abstract = "This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.",

keywords = "Cryoreduction, Cytochrome P450, Dioxygen activation, ENDOR, EPR, Heme oxygenase, Nitric oxide synthase",

author = "Roman Davydov and Hoffman, {Brian M.}",

note = "Funding Information: This work has been supported by the NIH (HL 13531, B.M.H.). It would not have been possible without the efforts of our many collaborators whose work is referenced. It further relied on the support of our colleagues, Mr. Clark Davoust and Dr. Peter Doan.",

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T1 - Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies

AU - Davydov, Roman

AU - Hoffman, Brian M.

N1 - Funding Information: This work has been supported by the NIH (HL 13531, B.M.H.). It would not have been possible without the efforts of our many collaborators whose work is referenced. It further relied on the support of our colleagues, Mr. Clark Davoust and Dr. Peter Doan.

PY - 2011/3/1

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N2 - This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.

AB - This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.

KW - Cryoreduction

KW - Cytochrome P450

KW - Dioxygen activation

KW - ENDOR

KW - EPR

KW - Heme oxygenase

KW - Nitric oxide synthase

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VL - 507

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JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

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Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies

Abstract

Keywords

ASJC Scopus subject areas

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