Structural evidence for a reaction intermediate mimic in the active site of a sulfite dehydrogenase.

Ahmed Djeghader, Melanie Rossotti, Saleh Abdulkarim, Frédéric Biaso, Guillaume Gerbaud, Wolfgang Nitschke, Barbara Schoepp-Cothenet, Tewfik Soulimane, Stéphane Grimaldi

Journal: Chemical communications (Cambridge, England) 2021;56(68):9850-9853

PMID: 32716419

Full Text on Royal Society of Chemistry View on PubMed

Abstract

By combining X-ray crystallography, electron paramagnetic resonance techniques and density functional theory-based modelling, we provide evidence for a direct coordination of the product analogue, phosphate, to the molybdenum active site of a sulfite dehydrogenase. This interaction is mimicking the still experimentally uncharacterized reaction intermediate proposed to arise during the catalytic cycle of this class of enzymes. This work opens new perspectives for further deciphering the reaction mechanism of this nearly ubiquitous class of oxidoreductases.

Address: Department of Chemical Sciences and Bernal Institute, University of Limerick, Ireland. [email protected].; Aix Marseille Univ, CNRS, BIP UMR7281, Marseille, France. [email protected] [email protected].

DOI: 10.1039/d0cc03634j

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MeSH Terms: Catalytic Domain, Crystallography, X-Ray, Density Functional Theory, Electron Spin Resonance Spectroscopy, Hydrogen Bonding, Molybdenum, Phosphates, Sulfite Dehydrogenase, Thermus