Functional Interactions in Cytochrome P450BM3: Flavin Semiquinone Intermediates, Role of NADP(H), and Mechanism of Electron Transfer by the Flavoprotein Domain-Reference-Cited by-同舟云学术

Functional Interactions in Cytochrome P450BM3: Flavin Semiquinone Intermediates, Role of NADP(H), and Mechanism of Electron Transfer by the Flavoprotein Domain

Published:1997-07-01 Issue:27 Volume:36 Page:8401-8412
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Murataliev Marat B.¹,Klein Michael¹,Fulco Armand¹,Feyereisen René¹

Affiliation:

1. Department of Entomology and Center for Toxicology, University of Arizona, Tucson, Arizona 85721-0036, and Department of Biological Chemistry, School of Medicine, University of California, Los Angeles, California 90095-1737

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi970026b

Reference56 articles.

1. Fatty acid monooxygenation by cytochrome P-450BM-3.

2. Reconstitution of the fatty acid hydroxylation function of cytochrome P-450BM-3 utilizing its individual recombinant hemo- and flavoprotein domains.

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