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    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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    Dalton_Spectroscopy-JHE-final2.pdf
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    Description:
    Final Accepted Manuscript
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    Author
    Enemark, John H
    Affiliation
    Univ Arizona, Dept Chem & Biochem
    Issue Date
    2017-10-21
    
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    Show full item record
    Publisher
    ROYAL SOC CHEMISTRY
    Citation
    Dalton Trans., 2017, 46, 13202
    Journal
    DALTON TRANSACTIONS
    Rights
    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 2017
    ISSN
    1477-9234
    PubMed ID
    28640289
    DOI
    10.1039/c7dt01731f
    Version
    Final accepted manuscript
    Additional Links
    https://pubs.rsc.org/en/content/articlehtml/2017/dt/c7dt01731f
    ae974a485f413a2113503eed53cd6c53
    10.1039/c7dt01731f
    Scopus Count
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