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Issue 39, 2017
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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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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.

Graphical abstract: 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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Publication details

The article was received on 12 May 2017, accepted on 14 Jun 2017 and first published on 14 Jun 2017


Article type: Paper
DOI: 10.1039/C7DT01731F
Citation: Dalton Trans., 2017,46, 13202-13210
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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

    J. H. Enemark, Dalton Trans., 2017, 46, 13202
    DOI: 10.1039/C7DT01731F

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