9xsa
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Crystal structure of a cupin protein (tm1459, R39M/H52A/H54A/H92A/C106E mutant) in ruthenium(p-cymene) bound form
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Structural highlights
FunctionPublication Abstract from PubMedA ruthenium(p-cymene)-cupin complex functioning as an artificial ketone reductase was developed through structure-guided engineering. Refinement of the primary and secondary coordination spheres based on a 1-His metal-binding motif enabled efficient asymmetric transfer hydrogenation of trifluoroacetophenone in water, affording up to 95% ee and 92% coupling efficiency. Rational design of a ruthenium-cupin complex as an artificial ketone reductase.,Matsumoto K, Kitazawa S, Matsumoto R, Morita Y, Fujieda N Chem Commun (Camb). 2026 Mar 17;62(21):5942-5946. doi: 10.1039/d5cc07188g. PMID:41769794[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 08:32, 29 April 2026.