Structural and Spectroscopic Investigations of pH-Dependent Mo(V) Species in a Bacterial Sulfite-Oxidizing Enzyme.
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DOI: 10.1021/acs.inorgchem.4c02584
Abstract: Mono-pyranopterin-containing sulfite-oxidizing enzymes (SOEs), including eukaryotic sulfite oxidases and homologous prokaryotic sulfite dehydrogenases (SDHs), are molybdenum enzymes that exist in almost all forms of life, where they catalyze the direct oxidation of sulfite into sulfate,… read more here.
Keywords: structural spectroscopic; investigations dependent; sulfite oxidizing; dependent species ... See more keywords
Consensus structures of the Mo(v) sites of sulfite-oxidizing enzymes derived from variable frequency pulsed EPR spectroscopy, isotopic labelling and DFT calculations.
Sign Up to like & getrecommendations! Published in 2017 at "Dalton transactions"
DOI: 10.1039/c7dt01731f
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… read more here.
Keywords: frequency pulsed; spectroscopy isotopic; sulfite oxidizing; oxidizing enzymes ... See more keywords