Dioxygen Inactivation of Pyruvate Formate-Lyase: EPR Evidence for the Formation of Protein-Based Sulfinyl and Peroxyl Radicals-Reference-Cited by-同舟云学术

Dioxygen Inactivation of Pyruvate Formate-Lyase: EPR Evidence for the Formation of Protein-Based Sulfinyl and Peroxyl Radicals

Published:1998-01-01 Issue:2 Volume:37 Page:558-563
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Reddy Sreelatha G.¹,Wong Kenny K.¹,Parast Camran V.¹,Peisach Jack¹,Magliozzo Richard S.¹,Kozarich John W.¹

Affiliation:

1. Department of Biochemistry, Merck Research Laboratories, Rahway, New Jersey 07065-0900, and Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi972086n

Reference31 articles.

1. The free radical of pyruvate formate-lyase. Characterization by EPR spectroscopy and involvement in catalysis as studied with the substrate-analogue hypopthosphite

2. Pyruvate Formate-Lyase of Escherichia coli: the Acetyl-Enzyme Intermediate

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