Pan, Hui-JieHuang, GangfengWodrich, Matthew D.Tirani, Farzaneh FadaeiAtaka, KenichiShima, SeigoHu, Xile2021-05-222021-05-222021-05-222021-05-0510.1002/anie.202100443https://infoscience.epfl.ch/handle/20.500.14299/178247WOS:000647231900001The reconstitution of [Mn]-hydrogenases using a series of Mn-I complexes is described. These complexes are designed to have an internal base or pro-base that may participate in metal-ligand cooperative catalysis or have no internal base or pro-base. Only Mn-I complexes with an internal base or pro-base are active for H-2 activation; only [Mn]-hydrogenases incorporating such complexes are active for hydrogenase reactions. These results confirm the essential role of metal-ligand cooperation for H-2 activation by the Mn-I complexes alone and by [Mn]-hydrogenases. Owing to the nature and position of the internal base or pro-base, the mode of metal-ligand cooperation in two active [Mn]-hydrogenases is different from that of the native [Fe]-hydrogenase. One [Mn]-hydrogenase has the highest specific activity of semi-synthetic [Mn]- and [Fe]-hydrogenases. This work demonstrates reconstitution of active artificial hydrogenases using synthetic complexes differing greatly from the native active site.Chemistry, MultidisciplinaryChemistrybiomimeticshydrogen activationhydrogenasemanganesemetal&#8211ligand cooperationtext::journal::journal article::research article