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Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex.

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第一作者： Jakob,Ruickoldt

第一单位： Department of Biochemistry, Institute of Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany.

作者： Jakob,Ruickoldt ^[1] ; Julian,Kreibich ^[2] ; Thomas,Bick ^[1] ; Jae-Hun,Jeoung ^[2] ; Benjamin R,Duffus ^[3] ; Silke,Leimkühler ^[3] ; Holger,Dobbek ^[2] ; Petra,Wendler ^[1]

作者单位： Department of Biochemistry, Institute of Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany. ^[1] Department of Biology, Humboldt-Universität zu Berlin, Berlin, Germany. ^[2] Department of Molecular Enzymology, Institute of Biochemistry and Biology, University of Potsdam, Potsdam-Golm, Germany. ^[3]

关键词 Biocatalysis Cryoelectron microscopy Enzyme mechanisms

DOI 10.1038/s41929-025-01365-y

PMID 40727002

发布时间 2025-07-31

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Nature catalysis

2025年8卷7期

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Nature catalysis

2025年8卷7期

657-667页

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Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex.

Nature catalysis

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Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex.

Nature catalysis

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