Consensus structures of the Mo(v) sites of sulfite-oxidizing enzymes derived from variable frequency pulsed EPR spectroscopy, isotopic labelling and DFT calculations-Reference-Cited by-同舟云学术

Consensus structures of the Mo(v) sites of sulfite-oxidizing enzymes derived from variable frequency pulsed EPR spectroscopy, isotopic labelling and DFT calculations

Published:2017 Issue:39 Volume:46 Page:13202-13210
ISSN:1477-9226
Container-title:Dalton Transactions
language:en
Short-container-title:Dalton Trans.

Author:

Enemark John H.¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry

2. University of Arizona

3. Tucson

4. USA

Abstract

The “blocked” form of sulfite oxidase has O-bound sulfite, and only the coordinated and remote O atoms exchange with H₂¹⁷O.

Publisher

Royal Society of Chemistry (RSC)

Subject

Inorganic Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/DT/C7DT01731F

Reference43 articles.

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2. Molybdenum and Tungsten Enzymes, ed. R. Hille, C. Schulzke and M. L. Kirk, The Royal Society of Chemistry, Cambridge, UK, 2017

3. The Mononuclear Molybdenum Enzymes

4. Investigation of the coordination structures of the molybdenum(v) sites of sulfite oxidizing enzymes by pulsed EPR spectroscopy

5. J. H. Enemark , A. V.Astashkin and A. M.Raitsimring, in Biological Magnetic Resonance, Volume 29. Metals in Biology: Applications of High Resolution EPR to Metalloenzymes, ed. G. R. Hanson and L. J. Berliner, 2010, ch. 6, pp. 122–168

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