Heme–thiolate sulfenylation of human cytochrome P450 4A11 functions as a redox switch for catalytic inhibition-Reference-Cited by-同舟云学术

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Heme–thiolate sulfenylation of human cytochrome P450 4A11 functions as a redox switch for catalytic inhibition

Published:2017-07 Issue:27 Volume:292 Page:11230-11242
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Albertolle Matthew E.,Kim Donghak,Nagy Leslie D.,Yun Chul-Ho,Pozzi Ambra,Savas Üzen,Johnson Eric F.,Guengerich F. Peter^ORCID

Funder

National Institutes of Health

National Research Foundation of Korea

U.S. Department of Veterans Affairs

American Heart Association

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference79 articles.

1. Cytochrome P450: Structure, Mechanism, and Biochemistry,2015

2. Human cytochrome P450 enzymes;Guengerich,2015

3. Arachidonic acid monooxygenase: genetic and biochemical approaches to physiological/pathophysiological relevance;Capdevila;Prostaglandins Other Lipid Mediat,2015

4. Kinetic analysis of lauric acid hydroxylation by human cytochrome P450 4A11;Kim;Biochemistry,2014

5. Formation of 20-hydroxyeicosatetraenoic acid, a vasoactive and natriuretic eicosanoid, in human kidney: role of Cyp4F2 and Cyp4A11;Lasker;J. Biol. Chem,2000

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