A Functional [NiFe]-Hydrogenase Model Compound That Undergoes Biologically Relevant Reversible Thiolate Protonation

作者：Weber Katharina; Kraemer Tobias; Shafaat Hannah S; Weyhermueller Thomas; Bill Eckhard; van Gastel Maurice; Neese Frank; Lubitz Wolfgang^*

来源：Journal of the American Chemical Society, 2012, 134(51): 20745-20755.

DOI：10.1021/ja309563p

Two model compounds of the active site of [NiFe]-hydrogenases with an unusual {S2Ni(mu-S)(mu-CO)Fe-(CO)(2)S}-coordination environment around the metals are reported. The neutral compound [Ni(xbsms)(mu-CO)(mu-S)Fe-(CO)(2)('S')], (1) (H(2)xbsms = 1,2-bis(4-mercapto-3,3-dimethyl-2-thiabutyl)benzene) is converted to [1H][BF4] by reversible protonation using HBF4 center dot Et2O. The protonation takes place at the terminal thiolate sulfur atom that is coordinated to nickel. Catalytic intermediates with a protonated terminal cysteinate were suggested for the native protein but have not yet been confirmed experimentally. [1H][BF4] is the first dinuclear [NiFe] model compound for such a species. Both complexes have been synthesized and characterized by X-ray crystallography, NMR-, FTIR-, and Fe-57-Mossbauer spectroscopy as well as by electronic absorption and resonance Raman spectroscopy. The experimental results clearly show that the protonation has a significant impact on the electronic structure of the iron center, although it takes place at the nickel site. DFT calculations support the interpretation of the spectroscopic data and indicate the presence of a bonding interaction between the metal ions, which is relevant for the enzyme as well. Electrochemical experiments show that both 1 and [1H][BF4] are active for electrocatalytic proton reduction in aprotic solvents.

• 出版日期2012-12-26