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Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic

2013; Nature Portfolio; Volume: 9; Issue: 10 Linguagem: Inglês

10.1038/nchembio.1311

1552-4469

Julian Esselborn, Camilla Lambertz, Agnieszka Adamska-Venkatesh, Trevor R. Simmons, Gustav Berggren, Jens Noth, Judith F. Siebel, Anja Hemschemeier, Vincent Artero, Edward J. Reijerse, Marc Fontecave, Wolfgang Lubitz, Thomas Happe,

Advanced battery technologies research

In cells, di-iron hydrogenases require three maturases to facilitate proper assembly of metal clusters. Reconstitution experiments with synthetic cofactor mimics coupled with functional and spectroscopic characterization now show these helper proteins are not needed in vitro to form highly active H2-producing catalysts. Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H2-producing catalysts.