Electron Paramagnetic Resonance and Electron-Nuclear Double Resonance Studies of the Reactions of Cryogenerated Hydroperoxoferric–Hemoprotein Intermediates-Reference-Cited by-同舟云学术

Electron Paramagnetic Resonance and Electron-Nuclear Double Resonance Studies of the Reactions of Cryogenerated Hydroperoxoferric–Hemoprotein Intermediates

Published:2014-07-21 Issue:30 Volume:53 Page:4894-4903
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Davydov Roman¹,Laryukhin Mikhail¹,Ledbetter-Rogers Amy²,Sono Masanori³,Dawson John H.³,Hoffman Brian M.¹

Affiliation:

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

2. Department of Chemistry and Biochemistry, College of Charleston, Charleston, South Carolina 29424, United States

3. Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina 29208, United States

Funder

Division of Molecular and Cellular Biosciences

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi500296d

Reference58 articles.

1. Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies

2. Hydroxylation of Camphor by Reduced Oxy-Cytochrome P450cam: Mechanistic Implications of EPR and ENDOR Studies of Catalytic Intermediates in Native and Mutant Enzymes

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

4. EPR and ENDOR Characterization of the Reactive Intermediates in the Generation of NO by Cryoreduced Oxy-Nitric Oxide Synthase from Geobacillus stearothermophilus

5. The Use of Deuterated Camphor as a Substrate in 1H ENDOR Studies of Hydroxylation by Cryoreduced Oxy P450cam Provides New Evidence of the Involvement of Compound I

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