Eric M. Shepard

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OBJECTIVE To develop clinical practice guidelines for the support of the patient and family in the adult, pediatric, or neonatal patient-centered ICU. PARTICIPANTS A multidisciplinary task force of experts in critical care practice was convened from the membership of the American College of Critical Care Medicine (ACCM) and the Society of Critical Care(More)
The organometallic H cluster at the active site of [FeFe]-hydrogenase consists of a 2Fe subcluster coordinated by cyanide, carbon monoxide, and a nonprotein dithiolate bridged to a [4Fe-4S] cluster via a cysteinate ligand. Biosynthesis of this cluster requires three accessory proteins, two of which (HydE and HydG) are radical S-adenosylmethionine enzymes.(More)
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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