Structural biology of redox partner interactions in P450cam monooxygenase: a fresh look at an old system.

doi:10.1016/j.abb.2010.08.022

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Article

Structural biology of redox partner interactions in P450cam monooxygenase: a fresh look at an old system.

Archives of biochemistry and biophysics - 1 Mar 2011

Sevrioukova Irina F, Poulos Thomas L

Abstract excerpt

The P450cam monooxygenase system consists of three separate proteins: the FAD-containing, NADH-dependent oxidoreductase (putidaredoxin reductase or Pdr), cytochrome P450cam and the 2Fe2S ferredoxin (putidaredoxin or Pdx), which transfers electrons from Pdr to P450cam. Over the past few years our lab has focused on the interaction between these redox components. It has been known for some time that Pdx can serve...

Topics

Animals
Bacterial Proteins
Camphor 5-Monooxygenase
Crystallography, X-Ray
Ferredoxins
Humans
Models, Molecular
Mutation
NADH, NADPH Oxidoreductases
Oxidation-Reduction
Protein Binding
Protein Conformation
Pseudomonas putida

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Identifiers

PMID: 20816746
DOI: 10.1016/j.abb.2010.08.022
PMCID: PMC3193999

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