E. Claude Hatchikian

TL;DR: The 2.54 Å resolution structure of Ni-Fe hydrogenase has revealed the existence of hydrophobic channels connecting the molecular surface to the active site, and a crystallographic analysis of xenon binding together with molecular dynamics simulations suggest that these channels serve as pathways for gas access to theactive site.

TL;DR: Volbeda et al. as discussed by the authors proposed a tentative assignment of these special groups to the three diatomic active site Fe ligands observed in the crystal structure of Desulfovibrio gigas hydrogenase based on their interaction with the protein environment.

TL;DR: Electrochemical redox titrations showed that the enzyme in the Hinact state converts to the transition state (Htrans) in a reversible one-electron redox step (Em, pH 7=–75 mV), and IR spectra demonstrate that the added redox equivalent not only affects the [4Fe-4S]H subcluster, but also the di-iron centre.

TL;DR: The results indicate that the activation of D. gigas hydrogenase does not involve conversions of a metal centre or the cleavage of an accessible disulphide bridge, and is suggested that a similar oxidation of the active enzyme may take place in the cell as a protection against oxygen.

TL;DR: A very stable enzymatic electrode is produced that catalyzes nonmediated H2 oxidation and is observed by the strong catalytic currents measured in the presence of the H2 substrate.