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January 27, 2010Angewandte Chemie International Edition157 citationsOpen Access

FeFe‐Hydrogenase Cyanide Ligands Derived From S ‐Adenosylmethionine‐Dependent Cleavage of Tyrosine

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RDRebecca C. DriesenerMCMartin R. ChallandSMShawn E. McGlynn

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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.

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Cite This Study

Driesener et al. (2010) studied this question.

synapsesocial.com/papers/6a5ea9955fa505cbb75fff7ahttps://doi.org/10.1002/anie.200907047
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