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Journal Article

A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor

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Huang,  Gangfeng
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Pan, H.-J., Huang, G., Wodrich, M. D., Tirani, F. F., Ataka, K., Shima, S., et al. (2019). A catalytically active [Mn]-hydrogenase incorporating a non-native metal cofactor. NATURE CHEMISTRY, 11(7), 669-675. doi:10.1038/s41557-019-0266-1.


Cite as: https://hdl.handle.net/21.11116/0000-0008-F2E2-7
Abstract
Nature carefully selects specific metal ions for incorporation into the enzymes that catalyse the chemical reactions necessary for life. Hydrogenases, enzymes that activate molecular H-2, exclusively utilize Ni and Fe in [NiFe]-, [FeFe]- and [Fe]-hydrogeanses. However, other transition metals are known to activate or catalyse the production of hydrogen in synthetic systems. Here, we report the development of a biomimetic model complex of [Fe]-hydrogenase that incorporates a Mn, as opposed to a Fe, metal centre. This Mn complex is able to heterolytically cleave H-2 as well as catalyse hydrogenation reactions. The incorporation of the model into an apoenzyme of [Fe]-hydrogenase results in a [Mn]-hydrogenase with an enhanced occupancy-normalized activity over an analogous semi-synthetic [Fe]-hydrogenase. These findings demonstrate a non-native metal hydrogenase that shows catalytic functionality and that hydrogenases based on a manganese active site are viable.