Hydroperoxy-Heme Oxygenase Generated by Cryoreduction Catalyzes the Formation of α-meso-Hydroxyheme as Detected by EPR and ENDOR-Reference-Cited by-同舟云学术

Hydroperoxy-Heme Oxygenase Generated by Cryoreduction Catalyzes the Formation of α-meso-Hydroxyheme as Detected by EPR and ENDOR

Published:1999-10-30 Issue:45 Volume:121 Page:10656-10657
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Davydov Roman M.¹,Yoshida Tadashi¹,Ikeda-Saito Masao¹,Hoffman Brian M.¹

Affiliation:

1. Department of Chemistry, Northwestern University Evanston, Illinois 60208 Department of Biochemistry Yamagata University School of Medicine Yamagata 990-9585, Japan Department of Physiology and Biophysics Case Western Reserve University School of Medicine Cleveland, Ohio 44106 Institute for Chemical Reaction Science 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/ja992425v

Reference25 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. Heme-Containing Oxygenases

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