1H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic 
Structure of the Active Site

Rumpel, Sigrun; Ravera, Enrico; Sommer, Constanze; Reijerse, Edward; Farès, Christophe; Luchinat, Claudio; Lubitz, Wolfgang

doi:10.1021/jacs.7b11196

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¹H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site

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Farès, Christophe
Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Rumpel, S., Ravera, E., Sommer, C., Reijerse, E., Farès, C., Luchinat, C., et al. (2018). ¹H NMR Spectroscopy of [FeFe] Hydrogenase: Insight into the Electronic Structure of the Active Site. Journal of the American Chemical Society, 140(1), 131-134. doi:10.1021/jacs.7b11196.

Cite as: https://hdl.handle.net/21.11116/0000-0001-63FA-6

Abstract

The [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii has been studied using ¹H NMR spectroscopy identifying the paramagnetically shifted ¹H resonances associated with both the [4Fe-4S]_H and the [2Fe]_H subclusters of the active site “H-cluster”. The signal pattern of the unmaturated HydA1 containing only [4Fe-4S]_H is reminiscent of bacterial-type ferredoxins. The spectra of maturated HydA1, with a complete H-cluster in the active H_ox and the CO-inhibited H_ox–CO state, reveal additional upfield and downfield shifted ¹H resonances originating from the four methylene protons of the azadithiolate ligand in the [2Fe]_H subsite. The two axial protons are affected by positive spin density, while the two equatorial protons experience negative spin density. These protons can be used as important probes sensing the effects of ligand-binding to the catalytic site of the H-cluster.