The active site structure and catalytic mechanism of arsenite oxidase

Scientific Reports
Thomas P WarelowGraham N George

Abstract

Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium sp. str. NT-26 using a combination of X-ray absorption spectroscopy and computational chemistry. Our analysis indicates an oxidized Mo(VI) active site with a structure that is far from equilibrium. We propose that this is an entatic state imposed by the protein on the active site through relative orientation of the two molybdopterin cofactors, in a variant of the Rây-Dutt twist of classical coordination chemistry, which we call the pterin twist hypothesis. We discuss the implications of this hypothesis for other putatively ancient molybdopterin-based enzymes.

References

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Citations

Apr 13, 2020·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Breeanna MintmierPartha Basu
Jul 4, 2020·Scientific Reports·Michael WellsJohn F Stolz
Aug 15, 2018·Proceedings of the National Academy of Sciences of the United States of America·Nathaniel R GlasserDianne K Newman

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Methods Mentioned

BETA
X-ray
gel-filtration

Software Mentioned

Materials Studio
Dmol
FEFF
BIOVIA Studio
EXAFSPAK

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