Catalytic Mechanism of Heme Oxygenase through EPR and ENDOR of Cryoreduced Oxy-Heme Oxygenase and Its Asp 140 Mutants-Reference-Cited by-同舟云学术

Catalytic Mechanism of Heme Oxygenase through EPR and ENDOR of Cryoreduced Oxy-Heme Oxygenase and Its Asp 140 Mutants

Published:2002-02-01 Issue:8 Volume:124 Page:1798-1808
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Davydov Roman¹,Kofman Viktoria¹,Fujii Hiroshi¹,Yoshida Tadashi¹,Ikeda-Saito Masao¹,Hoffman Brian M.¹

Affiliation:

1. Contribution from the Department of Chemistry, Northwestern University, Evanston, Illinois 60208, Institute for Molecular Science, Mydaiji, Okazaki 444-8585, Japan, Department of Biochemistry, Yamagata University School of Medicine, Yamagata 990-23, Japan, Department of Physiology and Biophysics, Case Western University School of Medicine, Cleveland, Ohio 44106-4970, and Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, Sendai 980-8577, Japan

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0122391

Reference38 articles.

1. Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species.

2. Heme Oxygenase Mechanism: Evidence for an Electrophilic, Ferric Peroxide Species

3. The Oxygen and Carbon Monoxide Reactions of Heme Oxygenase

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