Taming of a Poison: Biosynthesis of the NiFe-Hydrogenase Cyanide Ligands-Reference-Cited by-同舟云学术

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

Published:2003-02-14 Issue:5609 Volume:299 Page:1067-1070
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Reissmann Stefanie¹,Hochleitner Elisabeth²,Wang Haofan³,Paschos Athanasios¹,Lottspeich Friedrich²,Glass Richard S.³,Böck August¹

Affiliation:

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.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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