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      Cysteine SH and Glutamate COOH Contributions to [NiFe] Hydrogenase Proton Transfer Revealed by Highly Sensitive FTIR Spectroscopy

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          What vibrations tell about proteins

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            Theory of coupled electron and proton transfer reactions.

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              Hydrogens detected by subatomic resolution protein crystallography in a [NiFe] hydrogenase.

              The enzyme hydrogenase reversibly converts dihydrogen to protons and electrons at a metal catalyst. The location of the abundant hydrogens is of key importance for understanding structure and function of the protein. However, in protein X-ray crystallography the detection of hydrogen atoms is one of the major problems, since they display only weak contributions to diffraction and the quality of the single crystals is often insufficient to obtain sub-ångström resolution. Here we report the crystal structure of a standard [NiFe] hydrogenase (∼91.3 kDa molecular mass) at 0.89 Å resolution. The strictly anoxically isolated hydrogenase has been obtained in a specific spectroscopic state, the active reduced Ni-R (subform Ni-R1) state. The high resolution, proper refinement strategy and careful modelling allow the positioning of a large part of the hydrogen atoms in the structure. This has led to the direct detection of the products of the heterolytic splitting of dihydrogen into a hydride (H(-)) bridging the Ni and Fe and a proton (H(+)) attached to the sulphur of a cysteine ligand. The Ni-H(-) and Fe-H(-) bond lengths are 1.58 Å and 1.78Å, respectively. Furthermore, we can assign the Fe-CO and Fe-CN(-) ligands at the active site, and can obtain the hydrogen-bond networks and the preferred proton transfer pathway in the hydrogenase. Our results demonstrate the precise comprehensive information available from ultra-high-resolution structures of proteins as an alternative to neutron diffraction and other methods such as NMR structural analysis.
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                Author and article information

                Journal
                Angewandte Chemie International Edition
                Angew. Chem. Int. Ed.
                Wiley
                14337851
                August 13 2019
                Affiliations
                [1 ]Division of Materials Science; Graduate School of Science and Technology; Nara Institute of Science and Technology; 8916-5 Takayama, Ikoma Nara 630-0192 Japan
                [2 ]MOE Key Laboratory of Bioinorganic and Synthetic Chemistry; School of Chemistry; Sun Yat-Sen University; Guangzhou 510275 China
                [3 ]Graduate School of Life Science; University of Hyogo; 3-2-1 Koto Kamigori-cho, Ako-gun Hyogo 678-1297 Japan
                Article
                10.1002/anie.201904472
                31343102
                32bafe2d-ad06-40cd-82bd-23a873d4f204
                © 2019

                http://doi.wiley.com/10.1002/tdm_license_1.1

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