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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 transactions (Cambridge, England : 2003)

      Royal Society of Chemistry (RSC)

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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.

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          Author and article information

          Journal
          Dalton Trans
          Dalton transactions (Cambridge, England : 2003)
          Royal Society of Chemistry (RSC)
          1477-9234
          1477-9226
          Oct 10 2017
          : 46
          : 39
          Affiliations
          [1 ] Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85711, USA. jenemark@email.arizona.edu.
          Article
          10.1039/c7dt01731f
          28640289
          233ace17-6744-4655-85e2-3fa243c6bc67

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