Redox regulation of cytochrome P450cam mixed function oxidation by putidaredoxin and camphor ligation

I. C. Gunsalus; Stephen Sligar

doi:10.1016/S0300-9084(76)80364-1

Redox regulation of cytochrome P450_cam mixed function oxidation by putidaredoxin and camphor ligation

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

Abstract

A methylene group of camphor is hydroxylated by a P450 monoxygenase system containing in addition to the cytochrome and flavoprotein dehydrogenase a two-iron, two-sulfur redox protein termed putidaredoxin. The regulatory control of electron transport equilibrium occurs via ligation of substrate and redoxin to the cytochrome. The component interactions and electron flow are represented clearly and concisely by a free energy state diagram of the coupled binding and redox transfer reactions.

Original language	English (US)
Pages (from-to)	143-147
Number of pages	5
Journal	Biochimie
Volume	58
Issue number	1-2
DOIs	https://doi.org/10.1016/S0300-9084(76)80364-1
State	Published - Mar 12 1976

ASJC Scopus subject areas

Biochemistry

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title = "Redox regulation of cytochrome P450cam mixed function oxidation by putidaredoxin and camphor ligation",

abstract = "A methylene group of camphor is hydroxylated by a P450 monoxygenase system containing in addition to the cytochrome and flavoprotein dehydrogenase a two-iron, two-sulfur redox protein termed putidaredoxin. The regulatory control of electron transport equilibrium occurs via ligation of substrate and redoxin to the cytochrome. The component interactions and electron flow are represented clearly and concisely by a free energy state diagram of the coupled binding and redox transfer reactions.",

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AU - Sligar, Stephen

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N2 - A methylene group of camphor is hydroxylated by a P450 monoxygenase system containing in addition to the cytochrome and flavoprotein dehydrogenase a two-iron, two-sulfur redox protein termed putidaredoxin. The regulatory control of electron transport equilibrium occurs via ligation of substrate and redoxin to the cytochrome. The component interactions and electron flow are represented clearly and concisely by a free energy state diagram of the coupled binding and redox transfer reactions.

AB - A methylene group of camphor is hydroxylated by a P450 monoxygenase system containing in addition to the cytochrome and flavoprotein dehydrogenase a two-iron, two-sulfur redox protein termed putidaredoxin. The regulatory control of electron transport equilibrium occurs via ligation of substrate and redoxin to the cytochrome. The component interactions and electron flow are represented clearly and concisely by a free energy state diagram of the coupled binding and redox transfer reactions.

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