Search Results - "Jodts, Richard J."

The Elusive 5′-Deoxyadenosyl Radical: Captured and Characterized by Electron Paramagnetic Resonance and Electron Nuclear Double Resonance Spectroscopies by Yang, Hao, McDaniel, Elizabeth C, Impano, Stella, Byer, Amanda S, Jodts, Richard J, Yokoyama, Kenichi, Broderick, William E, Broderick, Joan B, Hoffman, Brian M

“…The 5′-deoxyadenosyl radical (5′-dAdo·) abstracts a substrate H atom as the first step in radical-based transformations catalyzed by…”
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A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis by Park, Yun Ji, Jodts, Richard J, Slater, Jeffrey W, Reyes, Reyvin M, Winton, Valerie J, Montaser, Rana A, Thomas, Paul M, Dowdle, William B, Ruiz, Anahi, Kelleher, Neil L, Bollinger, Jr, J Martin, Krebs, Carsten, Hoffman, Brian M, Rosenzweig, Amy C

“…SignificanceMethanobactins (Mbns), copper-binding peptidic compounds produced by some bacteria, are candidate therapeutics for human diseases of copper…”
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End-On Copper(I) Superoxo and Cu(II) Peroxo and Hydroperoxo Complexes Generated by Cryoreduction/Annealing and Characterized by EPR/ENDOR Spectroscopy by Davydov, Roman, Herzog, Austin E, Jodts, Richard J, Karlin, Kenneth D, Hoffman, Brian M

“…In this report, we investigate the physical and chemical properties of monocopper Cu­(I) superoxo and Cu­(II) peroxo and hydroperoxo complexes. These are…”
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Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the Cu C Site by EPR and ENDOR Spectroscopies by Jodts, Richard J, Ross, Matthew O, Koo, Christopher W, Doan, Peter E, Rosenzweig, Amy C, Hoffman, Brian M

“…In nature, methane is oxidized to methanol by two enzymes, the iron-dependent soluble methane monooxygenase (sMMO) and the copper-dependent particulate MMO…”
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Stern and Diffuse Layer Interactions during Ionic Strength Cycling by Ma, Emily, Kim, Jeongmin, Chang, HanByul, Ohno, Paul E, Jodts, Richard J, Miller, Thomas F, Geiger, Franz M

“…Second harmonic generation amplitude and phase measurements are acquired in real time from fused silica:water interfaces that are subjected to ionic strength…”
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Initial Steps in Methanobactin Biosynthesis: Substrate Binding by the Mixed-Valent Diiron Enzyme MbnBC by Jodts, Richard J., Ho, Madeline B., Reyes, Reyvin M., Park, Yun Ji, Doan, Peter E., Rosenzweig, Amy C., Hoffman, Brian M.

“…The MbnBC enzyme complex converts cysteine residues in a peptide substrate, MbnA, to oxazolone/thioamide groups during the biosynthesis of copper chelator…”
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Copper binding by a unique family of metalloproteins is dependent on kynurenine formation by Manesis, Anastasia C., Jodts, Richard J., Hoffman, Brian M., Rosenzweig, Amy C.

“…Some methane-oxidizing bacteria use the ribosomally synthesized, posttranslationally modified natural product methanobactin (Mbn) to acquire copper for their…”
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Characterization by ENDOR Spectroscopy of the Iron–Alkyl Bond in a Synthetic Counterpart of Organometallic Intermediates in Radical SAM Enzymes by Ho, Madeline B., Jodts, Richard J., Kim, Youngsuk, McSkimming, Alex, Suess, Daniel L. M., Hoffman, Brian M.

“…Members of the radical S-adenosyl-l-methionine (SAM) enzyme superfamily initiate a broad spectrum of radical transformations through reductive cleavage of SAM…”
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Mechanism of Radical S‑Adenosyl- l-methionine Adenosylation: Radical Intermediates and the Catalytic Competence of the 5′-Deoxyadenosyl Radical by Lundahl, Maike N, Sarksian, Raymond, Yang, Hao, Jodts, Richard J, Pagnier, Adrien, Smith, Donald F, Mosquera, Martín A, van der Donk, Wilfred A, Hoffman, Brian M, Broderick, William E, Broderick, Joan B

“…Radical S-adenosyl-l-methionine (SAM) enzymes employ a [4Fe–4S] cluster and SAM to initiate diverse radical reactions via either H-atom abstraction or…”
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Computational Description of Alkylated Iron–Sulfur Organometallic Clusters by Jodts, Richard J., Wittkop, M, Ho, Madeline B., Broderick, William E., Broderick, Joan B., Hoffman, Brian M., Mosquera, Martín A.

“…The radical S-adenosyl methionine (SAM) enzyme superfamily has widespread roles in hydrogen atom abstraction reactions of crucial biological importance. In…”
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Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the CuC Site by EPR and ENDOR Spectroscopies by Jodts, Richard J, Ross, Matthew O, Koo, Christopher W, Doan, Peter E, Rosenzweig, Amy C, Hoffman, Brian M

“…In nature, methane is oxidized to methanol by two enzymes, the iron-dependent soluble methane monooxygenase (sMMO) and the copper-dependent particulate MMO…”
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Active-Site Controlled, Jahn-Teller Enabled Regioselectivity in Reductive S-C Bond Cleavage of S -Adenosylmethionine in Radical SAM Enzymes by Impano, Stella, Yang, Hao, Jodts, Richard J, Pagnier, Adrien, Swimley, Ryan, McDaniel, Elizabeth C, Shepard, Eric M, Broderick, William E, Broderick, Joan B, Hoffman, Brian M

“…Catalysis by canonical radical -adenosyl-l-methionine (SAM) enzymes involves electron transfer (ET) from [4Fe-4S] to SAM, generating an R S radical that…”
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Spectroscopic and Computational Comparisons of Thiolate-Ligated Ferric Nonheme Complexes to Cysteine Dioxygenase: Second-Sphere Effects on Substrate (Analogue) Positioning by Fischer, Anne A, Miller, Joshua R, Jodts, Richard J, Ekanayake, Danushka M, Lindeman, Sergey V, Brunold, Thomas C, Fiedler, Adam T

“…Parallel spectroscopic and computational studies of iron­(III) cysteine dioxygenase (CDO) and synthetic models are presented. The synthetic complexes utilize…”
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Radical SAM Enzyme Spore Photoproduct Lyase: Properties of the Ω Organometallic Intermediate and Identification of Stable Protein Radicals Formed during Substrate-Free Turnover by Pagnier, Adrien, Yang, Hao, Jodts, Richard J, James, Christopher D, Shepard, Eric M, Impano, Stella, Broderick, William E, Hoffman, Brian M, Broderick, Joan B

“…Spore photoproduct lyase is a radical S-adenosyl-l-methionine (SAM) enzyme with the unusual property that addition of SAM to the [4Fe-4S]1+ enzyme absent…”
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Product analogue binding identifies the copper active site of particulate methane monooxygenase by Tucci, Frank J., Jodts, Richard J., Hoffman, Brian M., Rosenzweig, Amy C.

“…Nature’s primary methane-oxidizing enzyme, the membrane-bound particulate methane monooxygenase (pMMO), catalyses the oxidation of methane to methanol. Copper…”
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Active-Site Controlled, Jahn–Teller Enabled Regioselectivity in Reductive S–C Bond Cleavage of S -Adenosylmethionine in Radical SAM Enzymes by Impano, Stella, Yang, Hao, Jodts, Richard J., Pagnier, Adrien, Swimley, Ryan, McDaniel, Elizabeth C., Shepard, Eric M., Broderick, William E., Broderick, Joan B., Hoffman, Brian M.

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Stern and Diffuse Layer Interactions During Ionic Strength Cycling by Ma, Emily, Kim, Jeongmin, Chang, HanByul, Ohno, Paul E, Jodts, Richard J, MillerIII, Thomas F, Geiger, Franz M

“…Second harmonic generation amplitude and phase measurements are acquired in real time from fused silica:water interfaces that are subjected to ionic strength…”
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