Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron–Nuclear Double Resonance Spectroscopy-Reference-Cited by-同舟云学术

Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron–Nuclear Double Resonance Spectroscopy

Published:2016-02-03 Issue:6 Volume:55 Page:869-883
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Davydov Roman¹,Im Sangchoul²,Shanmugam Muralidharan¹,Gunderson William A.¹,Pearl Naw May²,Hoffman Brian M.¹,Waskell Lucy²

Affiliation:

1. Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208-3113, United States

2. Department of Anesthesiology, University of Michigan, and VA Medical Center, 2215 Fuller Road, Ann Arbor, Michigan 48105, United States

Funder

U.S. Department of Veterans Affairs

U.S. Department of Health and Human Services

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.5b00744

Reference78 articles.

1. Heme-Containing Oxygenases

2. Structure and Chemistry of Cytochrome P450

3. Catalysis by nitric oxide synthase

4. Revisiting Heme Mechanisms. A Perspective on the Mechanisms of Nitric Oxide Synthase (NOS), Heme Oxygenase (HO), and Cytochrome P450s (CYP450s)

5. Oxidizing species in the mechanism of cytochrome P450

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