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. 2003 Feb 14;299(5609):1067-70.
doi: 10.1126/science.1080972.

Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide ligands

Stefanie Reissmann  1 , Elisabeth Hochleitner, Haofan Wang, Athanasios Paschos, Friedrich Lottspeich, Richard S Glass, August Böck
Affiliations

Taming of a poison: biosynthesis of the NiFe-hydrogenase cyanide ligands

Stefanie Reissmann et al. Science. .

Abstract

NiFe-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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