- Apparently, the rate of inclusion for the FeFe core by HydF to HydA1 is the same as for the GTPase domain. And that rate is very similar to the GTPase of the NiFe family of hydrogenases.
- "However, it is interesting to note that a protein, with GTPase activity and Kd values for GTP comparable with those displayed by the TmHydF protein, is involved in the maturation of [Ni-Fe]-hydrogenase, which also contains a dinuclear metal site (consisting of a Ni atom and an Fe atom with CO and CN ligands). It has been shown that this protein, HypB, participates in the GTP-dependent insertion of the nickel atom into an hydrogenase form only containing the Fe(CO)(CN)2 motif (16). It is thus tempting to speculate that the HydF protein is also involved in the GTPase-driven insertion of the diiron complex, or part of it or of the [4Fe-4S] cluster to which the diiron complex binds, into the [Fe-Fe]-hydrogenase active site."
- doi: 10.1074/jbc.M510310200
- The planned Ferrodoxin from Synecosistis appears to be 100 times less efficient than the native one from R. etli. Therefore, we are not sure what would be the interest in adding it to our system. Check reference 30 of PNAS paper...
- This one