[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), 1687-1690. (doi:10.1002/anie.200907047).

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Description/Abstract

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.

Item Type: Article
ISSNs: 1521-3773 (electronic)
Related URLs:
Keywords: bioinorganic chemistry, biosynthesis, cyanides, hydrogenases, metalloenzymes
Subjects: Q Science > Q Science (General)
Divisions: University Structure - Pre August 2011 > School of Chemistry
Item ID: 146159
Date Deposited: 21 Apr 2010 11:47
Last Modified: 02 Mar 2012 12:35
Contributors: Driesener, Rebecca C. (Author)
Challand, Martin R. (Author)
McGlynn, Shawn E. (Author)
Shepard, Eric M. (Author)
Boyd, Eric S. (Author)
Broderick, Joan B. (Author)
Peters, John W. (Author)
Roach, Peter L. (Author)
Date: 27 January 2010
Status: Published
URI: http://eprints.soton.ac.uk/id/eprint/146159

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