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024 7 _ |a 10.1002/anie.202216903
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024 7 _ |a 1433-7851
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024 7 _ |a 0570-0833
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024 7 _ |a 1521-3773
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082 _ _ |a 540
100 1 _ |a Duan, Jifu
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245 _ _ |a Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway
260 _ _ |a Weinheim
|c 2023
|b Wiley-VCH
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520 _ _ |a Hydrogenases are H$_2$ converting enzymes that harbor catalytic cofactors in which iron (Fe) ions are coordinated by biologically unusual carbon monoxide (CO) and cyanide (CN$^–$) ligands. Extrinsic CO and CN$^–$, however, inhibit hydrogenases. The mechanism by which CN$^–$ binds to [FeFe]-hydrogenases is not known. Here, we obtained crystal structures of the CN$^–$-treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum. The high resolution of 1.39 Å allowed us to distinguish intrinsic CN$^–$ and CO ligands and to show that extrinsic CN$^–$ binds to the open coordination site of the cofactor where CO is known to bind. In contrast to other inhibitors, CN$^–$ treated crystals show conformational changes of conserved residues within the proton transfer pathway which could allow a direct proton transfer between E279 and S319. This configuration has been proposed to be vital for efficient proton transfer, but has never been observed structurally.
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700 1 _ |a Hemschemeier, Anja
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700 1 _ |a Burr, David J.
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700 1 _ |a Stripp, Sven T.
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700 1 _ |a Hofmann, Eckhard
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700 1 _ |a Happe, Thomas
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773 _ _ |a 10.1002/anie.202216903
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|t Angewandte Chemie / International edition
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856 4 _ |u https://onlinelibrary.wiley.com/doi/10.1002/anie.202216903
856 4 _ |u https://bib-pubdb1.desy.de/record/490284/files/Angew%20Chem%20Int%20Ed%20-%202022%20-%20Duan%20-%20Cyanide%20Binding%20to%20FeFe%20%E2%80%90Hydrogenase%20Stabilizes%20the%20Alternative%20Configuration%20of%20the.pdf
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