S K-edge XAS and DFT Calculations on Cytochrome P450: Covalent and Ionic Contributions to the Cysteine-Fe Bond and Their Contribution to Reactivity-Reference-Cited by-同舟云学术

S K-edge XAS and DFT Calculations on Cytochrome P450: Covalent and Ionic Contributions to the Cysteine-Fe Bond and Their Contribution to Reactivity

Published:2009-05-13 Issue:22 Volume:131 Page:7869-7878
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Dey Abhishek¹,Jiang Yonging¹,Ortiz de Montellano Paul¹,Hodgson Keith O.¹,Hedman Britt¹,Solomon Edward I.¹

Affiliation:

1. Department of Chemistry, Stanford University, Stanford, California 94305, Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, California 94025, and Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja901868q

Reference70 articles.

1. Structure and Chemistry of Cytochrome P450

2. Theoretical Perspective on the Structure and Mechanism of Cytochrome P450 Enzymes

3. Endogenous cysteine ligation in ferric and ferrous cytochrome P-450. Direct evidence from x-ray absorption spectroscopy.

4. Coupling of spin, substrate, and redox equilibriums in cytochrome P450

5. The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM

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