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[FeFe]-hydrogenase cyanide ligands derived FromS-adenosylmethionine-dependent cleavage of tyrosine

Driesener, Rebecca C., Challand, Martin R., McGlynn, Shawn E., Shepard, Eric M., Boyd, Eric S., Broderick, Joan B., Peters, John W. and Roach, Peter L. (2010) [FeFe]-hydrogenase cyanide ligands derived FromS-adenosylmethionine-dependent cleavage of tyrosine Angewandte Chemie International Edition, 49, (9), pp. 1687-1690. (doi:10.1002/anie.200907047).

Record type: Article


What's your poison?

Hydrogenases catalyze the reversible formation of dihydrogen from two electrons and two protons. The maturation of the [FeFe]-hydrogenase active-site cofactor (H cluster) requires three gene products, HydE, HydF, and HydG. Cyanide has been characterized as one of the products of tyrosine cleavage by the S-adenosylmethionine-dependent enzyme HydG, clarifying its role in H-cluster biosynthesis. DOA=deoxyadenosine.

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Published date: 27 January 2010
Keywords: bioinorganic chemistry, biosynthesis, cyanides, hydrogenases, metalloenzymes
Organisations: Chemistry


Local EPrints ID: 146159
ISSN: 1433-7851
PURE UUID: 8cc3e10b-9a48-4e21-a095-cff87abd69ab

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Date deposited: 21 Apr 2010 11:47
Last modified: 18 Jul 2017 23:04

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Author: Rebecca C. Driesener
Author: Martin R. Challand
Author: Shawn E. McGlynn
Author: Eric M. Shepard
Author: Eric S. Boyd
Author: Joan B. Broderick
Author: John W. Peters
Author: Peter L. Roach

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