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Membrane-Bound [NiFe]-Hydrogenase (MBH)

Lupe

The active site of [NiFe]-hydrogenases is composed of nickel and iron ions that are coordinated by four conserved cysteine ligands. The iron is additionally ligated by one carbonyl (CO) and two cyanide (CN-) groups. The hydrogenases of Ralstonia eutropha possess also this core structure of the catalytic center indicating that the special attribute of O2-tolerance relies on features that are in the vicinity or even remote of the active site.

We are interested in the individual properties that determine the O2 tolerance of [NiFe]-hydrogenases from Knallgas bacteria, and it turned out that nature has developed more than one solution.

The crystal structure of the membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha has been solved in collaboration with Patrick Scheerer and Christian Spahn (Charité Berlin). The proximal [4Fe-3S] cluster is surrounded by six cysteine ligands. This is in marked contrast to the canonical [4Fe4S] clusters that are coordinated by four cysteines. This feature leads to an unusual spatial and electronic structure of the cluster and is crucially related to the O2 tolerance of the enzyme.

 

 

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