Consensus structures of the Mo(v) sites of sulfite-oxidizing enzymes derived from variable frequency pulsed EPR spectroscopy, isotopic labelling and DFT calculations
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Final Accepted Manuscript
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Enemark, John HAffiliation
Univ Arizona, Dept Chem & BiochemIssue Date
2017-10-21
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ROYAL SOC CHEMISTRYCitation
Dalton Trans., 2017, 46, 13202Journal
DALTON TRANSACTIONSRights
This journal is © The Royal Society of Chemistry 2017.Collection Information
This item from the UA Faculty Publications collection is made available by the University of Arizona with support from the University of Arizona Libraries. If you have questions, please contact us at repository@u.library.arizona.edu.Abstract
Sulfite-oxidizing enzymes from eukaryotes and prokaryotes have five-coordinate distorted square-pyramidal coordination about the molybdenum atom. The paramagnetic Mo(v) state is easily generated, and over the years four distinct CW EPR spectra have been identified, depending upon enzyme source and the reaction conditions, namely high and low pH (hpH and lpH), phosphate inhibited (Pi) and sulfite (or blocked). Extensive studies of these paramagnetic forms of sulfite-oxidizing enzymes using variable frequency pulsed electron spin echo (ESE) spectroscopy, isotopic labeling and density functional theory (DFT) calculations have led to the consensus structures that are described here. Errors in some of the previously proposed structures are corrected.Note
12 month embargo; published online: 14 June 2017ISSN
1477-9234PubMed ID
28640289Version
Final accepted manuscriptAdditional Links
https://pubs.rsc.org/en/content/articlehtml/2017/dt/c7dt01731fae974a485f413a2113503eed53cd6c53
10.1039/c7dt01731f
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