Journal Article

PUBDB-2022-07617

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway

Duan, J. (Corresponding author)Extern*EMBL* ; Hemschemeier, A. ; Burr, D. J. ; Stripp, S. T. ; Hofmann, E. ; Happe, T. (Corresponding author)Extern*

2023
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/anie.202216903  doi:10.3204/PUBDB-2022-07617

Abstract: 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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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)
2. DFG project 390677874 - EXC 2033: RESOLV (Ruhr Explores Solvation) (390677874) (390677874)

Experiment(s):

1. PETRA Beamline P13 (PETRA III)
2. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2022

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Database coverage:
; ; ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 15 ; JCR ; Nationallizenz ; SCOPUS ; Web of Science Core Collection

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