6er9
Crystal structure of cyclohexanone monooxygenase from Rhodococcus sp. Phi1 bound to NADP+Crystal structure of cyclohexanone monooxygenase from Rhodococcus sp. Phi1 bound to NADP+
Structural highlights
Publication Abstract from PubMedMonoterpenoids offer potential as biocatalytically derived monomer feedstocks for high-performance renewable polymers. We describe a biocatalytic route to lactone monomers menthide and dihydrocarvide employing Baeyer-Villiger monooxygenases (BVMOs) from Pseudomonas sp. HI-70 (CPDMO) and Rhodococcus sp. Phi1 (CHMOPhi1) as an alternative to organic synthesis. The regioselectivity of dihydrocarvide isomer formation was controlled by site-directed mutagenesis of three key active site residues in CHMOPhi1. A combination of crystal structure determination, molecular dynamics simulations, and mechanistic modeling using density functional theory on a range of models provides insight into the origins of the discrimination of the wild type and a variant CHMOPhi1 for producing different regioisomers of the lactone product. Ring-opening polymerizations of the resultant lactones using mild metal-organic catalysts demonstrate their utility in polymer production. This semisynthetic approach utilizing a biocatalytic step, non-petroleum feedstocks, and mild polymerization catalysts allows access to known and also to previously unreported and potentially novel lactone monomers and polymers. Biocatalytic Routes to Lactone Monomers for Polymer Production.,Messiha HL, Ahmed ST, Karuppiah V, Suardiaz R, Ascue Avalos GA, Fey N, Yeates S, Toogood HS, Mulholland AJ, Scrutton NS Biochemistry. 2018 Apr 3;57(13):1997-2008. doi: 10.1021/acs.biochem.8b00169. Epub, 2018 Mar 22. PMID:29533655[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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