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Esselborn, Julian; Lambertz, Camilla; Adamska-Venkates, Agnieszka; Simmons, Trevor; Berggren, Gustav; Noth, Jens; Siebel, Judith; Hemschemeier, Anja; Artero, Vincent; Reijerse, Edward; Fontecave, Marc; Lubitz, Wolfgang; Happe, Thomas
Nature chemical biology, 10/2013, Letnik: 9, Številka: 10Journal Article
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.
