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Cofactor assembly and maturation of [NiFe]-hydrogenases

Model of the active site assembly of [NiFe]-hydrogenases. Six Hyp proteins are involved in synthesis of the cyanide ligands, their attachment to the iron atom and the insertion of the Ni and the Fe(CN)2 CO moiety into the apo-hydrogenase. The CN and CO li
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Assembly of the catalytic Ni-Fe center requires at least six accessory proteins involved in synthesis of the unique CO and CN- ligands and metal incorporation into the cofactor-free apo-hydrogenase. It is now quite established that the cyanide ligands are derived from carbamoyl phosphate, which also serves as central intermediate in the biosynthesis of arginine and DNA. The origin of the CO ligand, however, still needs to be unraveled.

We are using isotope labelled compounds, in order to test their incorporation into the diatomic ligands of the active site. The CO and CN- ligands can be identified on the basis of the characteristic absorption properties upon illumination with infrared light. Infrared absorption spectroscopy is done in collaboration with Ingo Zebger and Peter Hildebrandt at the Technical University of Berlin.

 

 

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