TU Berlin

Dr. Oliver LenzSH

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Dihydrogen-driven production of NADH by the soluble [NiFe]-hydrogenase

Current model of the SH from R. eutropha. The hydrogenase and diaphorase modules are drawn separately for sake of clarity. Main physiological reactions are shown in bold lines and fonts. Dotted lines in conjunction with a minus sign indicate product inhib

The NAD+-reducing soluble [NiFe]-hydrogenase (SH) of Ralstonia eutropha H16 couples H2 oxidation directly with the reduction NAD+ thereby providing the cells with reductant in the form of NADH. The enzyme is also capable in producing H2 as a result of NADH accumulation. Among the Ralstonia hydrogenases the SH is the most complex enzyme regarding both the subunit and cofactor composition. It consists of two independent catalytic moieties: a heterodimeric hydrogenase module (subunits HoxH and HoxY) containing the H2-converting [NiFe] center and a NADH:acceptor oxidoreductase module (or NAD+ reductase; subunits HoxF, HoxU and HoxI). Remarkably, the SH displays pronounced similarity the solvent-exposed arm of respiratory Complex I.

Because of the high complexity, we have investigated the individual catalytic modules independently in order to break the reaction mechanism of the SH into manageable parts. This research is carried out in cooperation with Kylie Vincent (Oxford University), Ingo Zebger / Friedhelm Lendzian / Peter Hildebrandt (Technische Universität Berlin) and Robert Bittl / Christian Teutloff (Freie Universität Berlin) and provided us with valuable insights into the molecular background of the catalytic mechanism and O2 tolerance of the enzyme.


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