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Science 14 February 2003:
Vol. 299. no. 5609, pp. 1067 - 1070
DOI: 10.1126/science.1080972
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Reports

Taming of a Poison: Biosynthesis of the NiFe-Hydrogenase Cyanide Ligands

Stefanie Reissmann,1 Elisabeth Hochleitner,2 Haofan Wang,3 Athanasios Paschos,1 Friedrich Lottspeich,2 Richard S. Glass,3 August Böck1*

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.

1 Department Biologie I, Mikrobiologie, University of Munich, Maria-Ward-Strasse 1a, D-80638 Munich, Germany.
2 Max-Planck Institut für Biochemie, Abteilung Proteinchemie, Am Klopferspitz, D-82152 Martinsried, Germany.
3 Department of Chemistry, University of Arizona, Post Office Box 210041, Tucson, AZ 85721-0041, USA.
*   To whom correspondence should be addressed. E-mail: august.boeck{at}lrz.uni-muenchen.de

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