[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).


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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
Digital Object Identifier (DOI): doi:10.1002/anie.200907047
ISSNs: 1433-7851 (print)
Related URLs:
Keywords: bioinorganic chemistry, biosynthesis, cyanides, hydrogenases, metalloenzymes
ePrint ID: 146159
Date :
Date Event
27 January 2010Published
Date Deposited: 21 Apr 2010 11:47
Last Modified: 18 Apr 2017 19:55
Further Information:Google Scholar
URI: http://eprints.soton.ac.uk/id/eprint/146159

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