Alcohol dehydrogenases can act as powerful catalysts in the preparation of optically pure γ-hydroxy-δ-lactones by means of an enantioconvergent dynamic redox isomerization of readily available Achmatowicz-type pyranones. Imitating the traditionally metal-mediated "borrowing hydrogen" approach to shuffle hydrides across molecular architectures and interconvert functional groups, this chemoinspired and purely biocatalytic interpretation effectively expands the enzymatic toolbox and provides new opportunities in the assembly of multienzyme cascades and tailor-made cellular factories.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6468324 | PMC |
http://dx.doi.org/10.1002/anie.201804911 | DOI Listing |
Nat Chem
January 2025
Instituto de Investigaciones Químicas, Consejo Superior de Investigaciones Científicas and Universidad de Sevilla, Sevilla, Spain.
Open-shell systems based on first-row transition metals and their involvement in various catalytic processes are well explored. By comparison, mononuclear open-shell complexes of precious transition metals remain underdeveloped. This is particularly true for Ir complexes, as there is very limited information available regarding their application in catalysis.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
Technische Universitat Dortmund, Chemistry and Chemical Biology, Otto-Hahn-Strasse 4a, 44227, Dortmund, GERMANY.
Iron-sulfur clusters play a crucial role in electron transfer for many essential enzymes, including [FeFe]-hydrogenases. This study focuses on the [4Fe4S] cluster ([4Fe]H) of the minimal [FeFe]-hydrogenase from Chlamydomonas reinhardtii (CrHydA1) and employs advanced spectroscopy, site-directed mutagenesis, molecular dynamics simulations, and QM/MM calculations. We provide insights into the complex electronic structure of [4Fe]H and its role in the catalytic reaction of CrHydA1, serving as paradigm for understanding [FeFe]-hydrogenases.
View Article and Find Full Text PDFJ Chem Phys
January 2025
Department of Chemistry and Biochemistry, University of Texas at El Paso, El Paso, Texas 79968, USA.
This study investigates the impact of structural isomerism on the excited state lifetime and redox energetics of heteroleptic [Ir(ppy)2(bpy)]+ and homoleptic Ir(ppy)3 photoredox catalysts using ground-state and time-dependent density functional theory methods. While the ground- and excited-state reduction potentials differ only slightly among the isomers of these complexes, our findings reveal significant variations in the radiative and non-radiative decay rates of the reactivity-controlling triplet 3MLCT states of these closely related species. The observed differences in radiative decay rates could be traced back to variations in the transition dipole moment, vertical energy gaps, and spin-orbit coupling of the isomers.
View Article and Find Full Text PDFChemistry
January 2025
Department of Chemistry, University of British Columbia, 2036 Main Mall, V6T 1Z1, Vancouver, BC, Canada.
The field of platinum chemistry is ubiquitous in the research of anticancer drugs and new OLED materials. Within the vast library of existing compounds, the majority of work focuses on complexes in the +2 and +4 oxidation states, with comparatively few examples of Pt complexes reported without bridging ligands. Pt complexes with metal-metal bonding can be made by mild oxidation of Pt complexes having bis(phenylpyridine) ligands.
View Article and Find Full Text PDFACS Chem Biol
January 2025
Professur Organische Chemie IV, Fakultät für Biologie, Chemie und Geowissenschaften, Department of Chemistry, Universität Bayreuth, 95447 Bayreuth, Germany.
Ketoreductases (KRs) are domains in the reductive loops of type I polyketide synthases (PKSs) and are responsible for the majority of stereocenters in reduced polyketides. Although the highly stereoselective reduction of ACP-bound β-ketothioester intermediates by KRs is crucial for the overall functioning of PKSs, the substrate-dependent stereoselectivity of KRs is a factor that is not yet fully understood, especially for KR domains in late PKS modules that act on biosynthetic precursors with complex polyketidic moieties. We present studies on the three KR domains FosKR7, PlmKR6, and EryKR6 from the biosynthetic pathways of fostriecin, phoslactomycin, and erythromycin by in vitro assays using close surrogates of the octaketidic FosKR7 biosynthetic precursor, complex derivatives and a diketide in the form of their biomimetic -acetylcysteamine thioesters.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!