Abstract
A series of [Mn]-hydrogenases were reconstituted using specifically designed MnI complexes. In two catalytically active [Mn]-hydrogenases, the mode of metal–ligand cooperation is different from that of the native [Fe]-hydrogenase. One such [Mn]-hydrogenase exhibits the highest specific activity among all known semi-synthetic [Mn]- and [Fe]-hydrogenases.
Highlights
Artificial enzymes incorporating non-native metal cofactors while exhibiting native activities can serve as important tools for mechanistic studies of enzymes.[1]
The mechanisms of H2 activation in previously reported [Fe]- and [Mn]-hydrogenases all involve metal-ligand cooperation, where a basic 2-OÀ group generated by deprotonation of the 2-OH group of an pyridone derivative deprotonates the H2 molecule coordinated to the metal ion (Figure 1 B).[1d,e,6a] In this study, we design and synthesize a series of MnI complexes with or without an internal base or pro-base (Figure 1 C)
Subsequent to the work with 1 a, we designed a series of new MnI models (1 b–1 e) that could be used to probe the influence of an internal base for H2 activation
Summary
Artificial enzymes incorporating non-native metal cofactors while exhibiting native activities can serve as important tools for mechanistic studies of enzymes.[1]. The mechanisms of H2 activation in previously reported [Fe]- and [Mn]-hydrogenases all involve metal-ligand cooperation, where a basic 2-OÀ group generated by deprotonation of the 2-OH group of an pyridone derivative deprotonates the H2 molecule coordinated to the metal ion (Figure 1 B).[1d,e,6a] In this study, we design and synthesize a series of MnI complexes with or without an internal base or pro-base (Figure 1 C). Among the former complexes, the nature and position of the internal base or pro-base are different. This strategy might be used to expand the functions of Hmd hydrogenases beyond native reactions using novel substrates other than methenyl-/methylene-H4MPT and H2
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