Probing Oxygen Activation Sites in Two Flavoprotein Oxidases Using Chloride as an Oxygen Surrogate-Reference-Cited by-同舟云学术

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Probing Oxygen Activation Sites in Two Flavoprotein Oxidases Using Chloride as an Oxygen Surrogate

Published:2011-05-26 Issue:24 Volume:50 Page:5521-5534
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Kommoju Phaneeswara-Rao¹,Chen Zhi-wei²,Bruckner Robert C.¹,Mathews F. Scott³,Jorns Marilyn Schuman¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102, United States

2. Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St. Louis, Missouri 63104, United States

3. Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200388g

Reference45 articles.

1. Activation of molecular oxygen by flavins and flavoproteins.

2. How Do Enzymes Activate Oxygen without Inactivating Themselves?

3. Detection of a C4a-Hydroperoxyflavin Intermediate in the Reaction of a Flavoprotein Oxidase

4. Oxygen Pressurized X-Ray Crystallography: Probing the Dioxygen Binding Site in Cofactorless Urate Oxidase and Implications for Its Catalytic Mechanism

5. Determination of the rate constant of self-exchange of the oxygen O2/O2- couple in water by 18O/16O isotope marking

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