Search Results - "Shepard, Eric M."
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Insights into [FeFe]-Hydrogenase Structure, Mechanism, and Maturation
Published in Structure (London) (10-08-2011)“…Hydrogenases are metalloenzymes that are key to energy metabolism in a variety of microbial communities. Divided into three classes based on their metal…”
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Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b
Published in The Journal of biological chemistry (16-03-2018)“…The H2O2-dependent oxidative decarboxylation of coproheme III is the final step in the biosynthesis of heme b in many microbes. However, the coproheme…”
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[FeFe]-Hydrogenase Cyanide Ligands Derived From S-Adenosylmethionine-Dependent Cleavage of Tyrosine
Published in Angewandte Chemie (International ed.) (22-02-2010)“…What's your poison? Hydrogenases catalyze the reversible formation of dihydrogen from two electrons and two protons. The maturation of the [FeFe]‐hydrogenase…”
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Biosynthesis of complex iron–sulfur enzymes
Published in Current opinion in chemical biology (01-04-2011)“…Recent advances in our understanding of the mechanisms for the biosynthesis of the complex iron–sulfur (Fe–S) containing prosthetic groups associated with…”
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Synthesis of the 2Fe subcluster of the [FeFe]-hydrogenase H cluster on the HydF scaffold
Published in Proceedings of the National Academy of Sciences - PNAS (08-06-2010)“…The organometallic H cluster at the active site of [FeFe]-hydrogenase consists of a 2Fe subcluster coordinated by cyanide, carbon monoxide, and a nonprotein…”
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Characterization of the Preprocessed Copper Site Equilibrium in Amine Oxidase and Assignment of the Reactive Copper Site in Topaquinone Biogenesis
Published in Journal of the American Chemical Society (05-06-2019)“…Copper-dependent amine oxidases produce their redox active cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ), via the CuII-catalyzed oxygenation of an…”
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EPR and FTIR Analysis of the Mechanism of H2 Activation by [FeFe]-Hydrogenase HydA1 from Chlamydomonas reinhardtii
Published in Journal of the American Chemical Society (08-05-2013)“…While a general model of H2 activation has been proposed for [FeFe]-hydrogenases, the structural and biophysical properties of the intermediates of the…”
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A shift between mineral and nonmineral sources of iron and sulfur causes proteome-wide changes in Methanosarcina barkeri
Published in Microbiology spectrum (06-02-2024)“…Iron (Fe) and sulfur (S) are required elements for life, and changes in their availability can limit the ecological distribution and function of…”
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Structure and Inhibition of Human Diamine Oxidase
Published in Biochemistry (Easton) (20-10-2009)“…Humans have three functioning genes that encode copper-containing amine oxidases. The product of the AOC1 gene is a so-called diamine oxidase (hDAO), named for…”
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HydF as a scaffold protein in [FeFe] hydrogenase H-cluster biosynthesis
Published in FEBS letters (25-06-2008)“…In an effort to determine the specific protein component(s) responsible for in vitro activation of the [FeFe] hydrogenase (HydA), the individual maturation…”
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Radical S‑Adenosylmethionine Enzymes
Published in Chemical reviews (23-04-2014)“…Broderick et al investigate radical s-adenosylmethionine (SAM) enzymes and detail their biochemical, structural and mechanistic elements. Strong reducing…”
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Inner-Sphere Mechanism for Molecular Oxygen Reduction Catalyzed by Copper Amine Oxidases
Published in Journal of the American Chemical Society (23-07-2008)“…Copper and topaquinone (TPQ) containing amine oxidases utilize O2 for the metabolism of biogenic amines while concomitantly generating H2O2 for use by the…”
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Identification and Characterization of a Novel Member of the Radical AdoMet Enzyme Superfamily and Implications for the Biosynthesis of the Hmd Hydrogenase Active Site Cofactor
Published in Journal of Bacteriology (01-01-2010)“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation
Published in Biochimica et biophysica acta (01-06-2015)“…The [FeFe]- and [NiFe]-hydrogenases catalyze the formal interconversion between hydrogen and protons and electrons, possess characteristic non-protein ligands…”
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[FeFe]‐Hydrogenase In Vitro Maturation
Published in Angewandte Chemie (International ed.) (05-12-2022)“…The [FeFe]‐hydrogenase H‐cluster is a complex organometallic cofactor whose assembly and installation requires three dedicated accessory proteins referred to…”
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Inhibition and Oxygen Activation in Copper Amine Oxidases
Published in Accounts of chemical research (19-05-2015)“…Copper-containing amine oxidases (CuAOs) use both copper and 2,4,5-trihydroxyphenylalanine quinone (TPQ) to catalyze the oxidative deamination of primary…”
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Intramolecular electron transfer rate between active-site copper and TPQ in Arthrobacter globiformis amine oxidase
Published in Journal of biological inorganic chemistry (01-11-2006)“…Copper amine oxidases catalyze the oxidative deamination of primary amines operating through a ping-pong bi bi mechanism, divided into reductive and oxidative…”
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Role of ammonia-lyases in the synthesis of the dithiomethylamine ligand during [FeFe]-hydrogenase maturation
Published in The Journal of biological chemistry (01-10-2024)“…The generation of an active [FeFe]-hydrogenase requires the synthesis of a complex metal center, the H-cluster, by three dedicated maturases: the radical…”
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S -Adenosyl-l-ethionine is a Catalytically Competent Analog of S -Adenosyl-l-methione (SAM) in the Radical SAM Enzyme HydG
Published in Angewandte Chemie International Edition (23-02-2021)“…Radical S-adenosyl-l-methionine (SAM) enzymes initiate biological radical reactions with the 5'-deoxyadenosyl radical (5'-dAdo•). A [4Fe-4S] cluster…”
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Photoinduced Electron Transfer in a Radical SAM Enzyme Generates an S‑Adenosylmethionine Derived Methyl Radical
Published in Journal of the American Chemical Society (09-10-2019)“…Radical SAM (RS) enzymes use S-adenosyl-l-methionine (SAM) and a [4Fe–4S] cluster to initiate a broad spectrum of radical transformations throughout all…”
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