A [RuRu] Analogue of an [FeFe]-Hydrogenase Traps the Key Hydride Intermediate of the Catalytic Cycle.

Autor: Sommer C; Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470, Mülheim an der Ruhr, Germany., Richers CP; School of Chemical Sciences, University of Illinois at Urbana-Champaign, 600 S. Goodwin Ave., Urbana, IL, 61801, USA., Lubitz W; Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470, Mülheim an der Ruhr, Germany., Rauchfuss TB; School of Chemical Sciences, University of Illinois at Urbana-Champaign, 600 S. Goodwin Ave., Urbana, IL, 61801, USA., Reijerse EJ; Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470, Mülheim an der Ruhr, Germany.
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2018 May 04; Vol. 57 (19), pp. 5429-5432. Date of Electronic Publication: 2018 Mar 26.
DOI: 10.1002/anie.201801914
Abstrakt: The active site of the [FeFe]-hydrogenases features a binuclear [2Fe] H sub-cluster that contains a unique bridging amine moiety close to an exposed iron center. Heterolytic splitting of H 2 results in the formation of a transient terminal hydride at this iron site, which, however is difficult to stabilize. We show that the hydride intermediate forms immediately when [2Fe] H is replaced with [2Ru] H analogues through artificial maturation. Outside the protein, the [2Ru] H analogues form bridging hydrides, which rearrange to terminal hydrides after insertion into the apo-protein. H/D exchange of the hydride only occurs for [2Ru] H analogues containing the bridging amine moiety.
(© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Databáze: MEDLINE
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