Journal
NATURE CHEMISTRY
Volume 13, Issue 4, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41557-020-00633-7
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Funding
- NIH [S10OD023532, R37 GM130387]
- Office of Science, of the US Department of Energy [DEAC02-05CH11231]
- Miller Institute for Basic Research in Science at the University of California Berkeley
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Research has shown that zinc-containing carbonic anhydrase enzymes can efficiently catalyze hydride transfers from silanes to ketones, involving a mononuclear zinc hydride in the process, and demonstrating that abiotic silanes can act as reducing equivalents in enzyme-catalyzed reactions. This work bridges the gap between the types of transformations in molecular catalysis and biocatalysis.
Enzymatic reactions through mononuclear metal hydrides are unknown in nature, despite the prevalence of such intermediates in the reactions of synthetic transition-metal catalysts. If metalloenzymes could react through abiotic intermediates like these, then the scope of enzyme-catalysed reactions would expand. Here we show that zinc-containing carbonic anhydrase enzymes catalyse hydride transfers from silanes to ketones with high enantioselectivity. We report mechanistic data providing strong evidence that the process involves a mononuclear zinc hydride. This work shows that abiotic silanes can act as reducing equivalents in an enzyme-catalysed process and that monomeric hydrides of electropositive metals, which are typically unstable in protic environments, can be catalytic intermediates in enzymatic processes. Overall, this work bridges a gap between the types of transformation in molecular catalysis and biocatalysis.
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