The University of Southampton
University of Southampton Institutional Repository

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

[FeFe]-hydrogenase cyanide ligands derived FromS-adenosylmethionine-dependent cleavage of tyrosine
[FeFe]-hydrogenase cyanide ligands derived FromS-adenosylmethionine-dependent cleavage of tyrosine
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.
bioinorganic chemistry, biosynthesis, cyanides, hydrogenases, metalloenzymes
1433-7851
1687-1690
Driesener, Rebecca C.
a42528a9-1225-4246-acca-095b99cc9d3e
Challand, Martin R.
03bb1ded-9274-4525-8377-8e5930f30d65
McGlynn, Shawn E.
894be6e2-ef61-43f4-b3fa-077afd7735cb
Shepard, Eric M.
2f916a0e-62bf-410b-bf52-b0756e86365e
Boyd, Eric S.
049410ba-5542-4cd7-868e-10e58702d46a
Broderick, Joan B.
9eb68505-070d-4ba2-a2ad-71c942330a1a
Peters, John W.
84377e0f-e6d8-4e56-aed8-584ec85c28ad
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9
Driesener, Rebecca C.
a42528a9-1225-4246-acca-095b99cc9d3e
Challand, Martin R.
03bb1ded-9274-4525-8377-8e5930f30d65
McGlynn, Shawn E.
894be6e2-ef61-43f4-b3fa-077afd7735cb
Shepard, Eric M.
2f916a0e-62bf-410b-bf52-b0756e86365e
Boyd, Eric S.
049410ba-5542-4cd7-868e-10e58702d46a
Broderick, Joan B.
9eb68505-070d-4ba2-a2ad-71c942330a1a
Peters, John W.
84377e0f-e6d8-4e56-aed8-584ec85c28ad
Roach, Peter L.
ca94060c-4443-482b-af3e-979243488ba9

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).

Record type: Article

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.

Full text not available from this repository.

More information

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

Identifiers

Local EPrints ID: 146159
URI: http://eprints.soton.ac.uk/id/eprint/146159
ISSN: 1433-7851
PURE UUID: 8cc3e10b-9a48-4e21-a095-cff87abd69ab
ORCID for Peter L. Roach: ORCID iD orcid.org/0000-0001-9880-2877

Catalogue record

Date deposited: 21 Apr 2010 11:47
Last modified: 17 Dec 2019 01:52

Export record

Altmetrics

Contributors

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 ORCID iD

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×