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

Author:

Enemark John H.1234ORCID

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

Reference43 articles.

1. Equilibria amongst different molybdenum (V)-containing species from sulphite oxidase. Evidence for a halide ligand of molybdenum in the low-pH species

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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