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- Stefanie Reissmann, Elisabeth Hochleitner, Haofan Wang, Athanasios Paschos, Friedrich Lottspeich, Richard S Glass, and August Böck.
- Department Biologie I, Mikrobiologie, University of Munich, Maria-Ward-Strasse 1a, D-80638 Munich, Germany.
- Science. 2003 Feb 14; 299 (5609): 1067-70.
AbstractNiFe-hydrogenases have an Ni-Fe site in which the iron has one CO and two CN groups as ligands. Synthesis of the CN ligands requires the activity of two hydrogenase maturation proteins: HypF and HypE. HypF is a carbamoyltransferase that transfers the carbamoyl moiety of carbamoyladenylate to the COOH-terminal cysteine of HypE and thus forms an enzyme-thiocarbamate. HypE dehydrates the S-carbamoyl moiety in an adenosine triphosphate-dependent process to yield the enzyme thiocyanate. Chemical model reactions corroborate the feasibility of this unprecedented biosynthetic route and show that thiocyanates can donate CN to iron. This finding underscores a striking parallel between biochemistry and organometallic chemistry in the formation of an iron-cyano complex.
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