The Structure of Formaldehyde-Inhibited Xanthine Oxidase Determined by 35 GHz 2H ENDOR Spectroscopy-Reference-Cited by-同舟云学术

The Structure of Formaldehyde-Inhibited Xanthine Oxidase Determined by 35 GHz 2H ENDOR Spectroscopy

Published:2010-09-22 Issue:40 Volume:132 Page:14015-14017
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Shanmugam Muralidharan¹,Zhang Bo¹,McNaughton Rebecca L.¹,Kinney R. Adam¹,Hille Russ¹,Hoffman Brian M.¹

Affiliation:

1. Chemistry Department, Northwestern University, Evanston, Illinois 60208-3113, and Department of Biochemistry, University of California, Riverside, California 95521

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja106432h

Reference25 articles.

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2. Hille, R.InMetals in Biology: Applications of High-Resolution EPR to Metalloenzymes;Hanson, G. and Berliner, L., Eds.Biological Magnetic Resonance, Vol. 29;Springer:Berlin, 2010; pp91−121.

3. Reaction of Formaldehyde and of Methanol with Xanthine Oxidase

4. 13C-ENDOR Studies of the Inhibited Species of Xanthine Oxidase: The First Direct Evidence for a Molybdenum-Carbon Bond in a Biological System

5. Evidence Favoring Molybdenum−Carbon Bond Formation in Xanthine Oxidase Action: 17O- and 13C-ENDOR and Kinetic Studies

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