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PMID: 2993062 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Electron-paramagnetic-resonance studies using pre-steady-state kinetics and substitution with stable isotopes on the mechanism of action of molybdoenzymes.

Biochemical Society transactions ·Vol. 13 ·No. 3 ·1985-06-00 ·Pages 560-7

Bray RC, George GN

Abstract

暂无摘要

MeSH Terms

Animals Electron Spin Resonance Spectroscopy/methods Freezing Kinetics Metalloproteins/metabolism Oxidation-Reduction Protein Conformation Thermodynamics Xanthine Xanthine Oxidase/metabolism Xanthines/metabolism

Chemicals

Metalloproteins Xanthines Xanthine Xanthine Oxidase

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Bray R C

George G N

Article Info

Journal

Biochemical Society transactions

Abbr.

Biochem Soc Trans

ISSN

0300-5127

DOI

10.1042/bst0130560

Published

1985-06-00

Pages

560-7

Language

English

Region

England

NLM ID

7506897

Subset

External Links

PubMed source DOI: 10.1042/bst0130560 View journal details

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Electron-paramagnetic-resonance studies using pre-steady-state kinetics and substitution with stable isotopes on the mechanism of action of molybdoenzymes.

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