Eric M. Shepard

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The organometallic H-cluster at the active site of the [FeFe]-hydrogenase serves as the site of reversible binding and reduction of protons to produce H2. The H-cluster is unique in biology, and consists of a 2Fe subcluster tethered to a typical [4Fe–4S] cluster by a single cysteine ligand. The remaining ligands to the 2Fe subcluster include three carbon(More)
Spore photoproduct lyase (SPL), a member of the radical S-adenosyl-l-methionine (SAM) superfamily, catalyzes the direct reversal of the spore photoproduct, a thymine dimer specific to bacterial spores, to two thymines. SPL requires SAM and a redox-active [4Fe–4S] cluster for catalysis. Mössbauer analysis of anaerobically purified SPL indicates the presence(More)
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