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Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2017-03-20 , DOI: 10.1021/jacs.7b00686 Edward J Reijerse 1 , Cindy C Pham 2 , Vladimir Pelmenschikov 3 , Ryan Gilbert-Wilson 4 , Agnieszka Adamska-Venkatesh 1 , Judith F Siebel 1 , Leland B Gee 2 , Yoshitaka Yoda 5 , Kenji Tamasaku 5 , Wolfgang Lubitz 1 , Thomas B Rauchfuss 4 , Stephen P Cramer 2
Journal of the American Chemical Society ( IF 14.4 ) Pub Date : 2017-03-20 , DOI: 10.1021/jacs.7b00686 Edward J Reijerse 1 , Cindy C Pham 2 , Vladimir Pelmenschikov 3 , Ryan Gilbert-Wilson 4 , Agnieszka Adamska-Venkatesh 1 , Judith F Siebel 1 , Leland B Gee 2 , Yoshitaka Yoda 5 , Kenji Tamasaku 5 , Wolfgang Lubitz 1 , Thomas B Rauchfuss 4 , Stephen P Cramer 2
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[FeFe]-hydrogenases catalyze the reversible reduction of protons to molecular hydrogen with extremely high efficiency. The active site ("H-cluster") consists of a [4Fe-4S]H cluster linked through a bridging cysteine to a [2Fe]H subsite coordinated by CN- and CO ligands featuring a dithiol-amine moiety that serves as proton shuttle between the protein proton channel and the catalytic distal iron site (Fed). Although there is broad consensus that an iron-bound terminal hydride species must occur in the catalytic mechanism, such a species has never been directly observed experimentally. Here, we present FTIR and nuclear resonance vibrational spectroscopy (NRVS) experiments in conjunction with density functional theory (DFT) calculations on an [FeFe]-hydrogenase variant lacking the amine proton shuttle which is stabilizing a putative hydride state. The NRVS spectra unequivocally show the bending modes of the terminal Fe-H species fully consistent with widely accepted models of the catalytic cycle.
中文翻译：
通过核共振振动光谱直接观察 [FeFe]-氢化酶中的铁结合末端氢化物
[FeFe]-氢化酶以极高的效率催化质子可逆还原为分子氢。活性位点（“H-簇”）由一个 [4Fe-4S]H 簇组成，该簇通过桥连半胱氨酸连接到由 CN- 和 CO 配体协调的 [2Fe]H 亚位点，其特征是二硫醇胺部分充当质子穿梭机蛋白质质子通道和催化远端铁位点 (Fed) 之间。尽管人们普遍认为催化机制中必须存在铁结合的末端氢化物物质，但这种物质从未在实验中直接观察到。在这里，我们展示了 FTIR 和核共振振动光谱 (NRVS) 实验以及密度泛函理论 (DFT) 计算，对缺乏稳定假定氢化物状态的胺质子穿梭的 [FeFe]-氢化酶变体进行了计算。 NRVS 光谱明确显示了末端 Fe-H 物质的弯曲模式，与广泛接受的催化循环模型完全一致。
更新日期：2017-03-20
中文翻译：
通过核共振振动光谱直接观察 [FeFe]-氢化酶中的铁结合末端氢化物
[FeFe]-氢化酶以极高的效率催化质子可逆还原为分子氢。活性位点（“H-簇”）由一个 [4Fe-4S]H 簇组成，该簇通过桥连半胱氨酸连接到由 CN- 和 CO 配体协调的 [2Fe]H 亚位点，其特征是二硫醇胺部分充当质子穿梭机蛋白质质子通道和催化远端铁位点 (Fed) 之间。尽管人们普遍认为催化机制中必须存在铁结合的末端氢化物物质，但这种物质从未在实验中直接观察到。在这里，我们展示了 FTIR 和核共振振动光谱 (NRVS) 实验以及密度泛函理论 (DFT) 计算，对缺乏稳定假定氢化物状态的胺质子穿梭的 [FeFe]-氢化酶变体进行了计算。 NRVS 光谱明确显示了末端 Fe-H 物质的弯曲模式，与广泛接受的催化循环模型完全一致。
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