Journal
CHEMICAL COMMUNICATIONS
Volume 56, Issue 68, Pages 9850-9853Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0cc03634j
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Funding
- Aix Marseille Univ
- CNRS
- Libyan ministry of higher education and scientific research
- IR CNRS [3443]
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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.
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