Fig. 7 In the oval are the cofactors of [Fe]-H 2 ase, collectively Hmd, the catalyst for hydrogen
splitting and hydride addition to the substrate, C 14 -H 4 MPT
+ , yielding reduced product C 14 -H 4 MPT
Fig. 8 Structure (1) truncated version of [Fe]-H 2 ase active site; [65]. (2) An iron model faithful to
the first coordination sphere of the active site; [77]. (3) An acyl-manganese analogue inspired by
the [Fe]-H 2 ase active site [78]. (4) Rose’s anthracene platform [79]. (5) Hu and Shima’s Fe-model
used in hybrid enzyme preparations [80]
Organometallic Chemistry Control of Hydrogenases
283
splitting and hydride addition to the substrate, C 14 -H 4 MPT
+ , yielding reduced product C 14 -H 4 MPT
Fig. 8 Structure (1) truncated version of [Fe]-H 2 ase active site; [65]. (2) An iron model faithful to
the first coordination sphere of the active site; [77]. (3) An acyl-manganese analogue inspired by
the [Fe]-H 2 ase active site [78]. (4) Rose’s anthracene platform [79]. (5) Hu and Shima’s Fe-model
used in hybrid enzyme preparations [80]
Organometallic Chemistry Control of Hydrogenases
283