[FeFe] -hydrogenase is a metalloenzyme involved in the microbial energy metabolism of various bacteria and algae, and has extremely strong catalytic performance, if it can be converted into a means of generating and using hydrogen in fuel cells Will be extremely useful. In these enzymes, the catalysis occurs at a unique "two iron" center, which contains a bridged "dithiolate" ligand, three CO ligands and two CN ligands. In this paper, the authors found that the three synthetic mimetics of this "two iron" center can be loaded onto the [FeFe] -hydrogenase mature protein HydF and then transferred to the algae variant apo-HydA1. Full activation of HydA1 can only be achieved by the HydF hybrid protein containing a mimic of an "azadithiolate" bridge, thus confirming the presence of this ligand at the active site of native [FeFe] -hydrogenase. This is the first example of using a specific protein scaffold in combination with a synthetic analogue of active sites to achieve controlled metalloenzyme activation.
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