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

I. C. Gunsalus, Stephen Sligar

Research output: Contribution to journalArticlepeer-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 languageEnglish (US)
Pages (from-to)143-147
Number of pages5
JournalBiochimie
Volume58
Issue number1-2
DOIs
StatePublished - Mar 12 1976

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Redox regulation of cytochrome P450<sub>cam</sub> mixed function oxidation by putidaredoxin and camphor ligation'. Together they form a unique fingerprint.

Cite this