Výsledky vyhledávání - "Richard J Jodts"

Characterization by ENDOR Spectroscopy of the Iron–Alkyl Bond in a Synthetic Counterpart of Organometallic Intermediates in Radical SAM Enzymes

Autor: Madeline B. Ho, Richard J. Jodts, Youngsuk Kim, Alex McSkimming, Daniel L. M. Suess, Brian M. Hoffman

Publikováno v: J Am Chem Soc

Members of the radical S-adenosyl-l-methionine (SAM) enzyme superfamily initiate a broad spectrum of radical transformations through reductive cleavage of SAM by a [4Fe−4S](1+) cluster it coordinates, to generate the reactive 5’-deoxyadenosyl rad

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba02041dec077933e4eb94b899addf8a
https://doi.org/10.1021/jacs.2c07155

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Mechanism of Radical S-Adenosyl-l-methionine Adenosylation: Radical Intermediates and the Catalytic Competence of the 5′-Deoxyadenosyl Radical

Autor: Maike N. Lundahl, Raymond Sarksian, Hao Yang, Richard J. Jodts, Adrien Pagnier, Donald F. Smith, Martín A. Mosquera, Wilfred A. van der Donk, Brian M. Hoffman, William E. Broderick, Joan B. Broderick

Publikováno v: J Am Chem Soc

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 substrate adenosylation. Here we use freeze-quench techniques together with electron paramagnetic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92f296f42bf01a118596f0ade76f89d4
https://doi.org/10.1021/jacs.1c13706

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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

Autor: Peter E. Doan, Amy C. Rosenzweig, Brian M. Hoffman, Christopher W. Koo, Matthew O. Ross, Richard J. Jodts

Publikováno v: Journal of the American Chemical Society. 143:15358-15368

In nature, methane is oxidized to methanol by two enzymes, the iron-dependent soluble methane monooxygenase (sMMO) and the copper-dependent particulate MMO (pMMO). While sMMO's diiron metal active site is spectroscopically and structurally well-chara

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6221be8aa105ba32baeb5e97b2270b8b
https://doi.org/10.1021/jacs.1c07018

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Stern and Diffuse Layer Interactions during Ionic Strength Cycling

Autor: Thomas F. Miller, Jeongmin Kim, Richard J. Jodts, Emily Ma, Franz M. Geiger, Paul E. Ohno, HanByul Chang

Publikováno v: The Journal of Physical Chemistry C. 125:18002-18014

Second harmonic generation amplitude and phase measurements are acquired in real time from fused silica:water interfaces that are subjected to ionic strength transitions conducted at pH 5.8. In conjunction with atomistic modeling, we identify correla

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a64270a3d1236ccdb264ce924e151bae
https://doi.org/10.1021/acs.jpcc.1c04836

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Active-Site Controlled, Jahn–Teller Enabled Regioselectivity in Reductive S–C Bond Cleavage of S-Adenosylmethionine in Radical SAM Enzymes

Autor: Eric M. Shepard, Hao Yang, Ryan Swimley, William E. Broderick, Joan B. Broderick, Richard J. Jodts, Stella Impano, Elizabeth C. McDaniel, Adrien Pagnier, Brian M. Hoffman

Publikováno v: Journal of the American Chemical Society. 143:335-348

Catalysis by canonical radical S-adenosyl-l-methionine (SAM) enzymes involves electron transfer (ET) from [4Fe-4S]+ to SAM, generating an R3S0 radical that undergoes regioselective homolytic reductive cleavage of the S-C5' bond to generate the 5'-dAd

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::149114bf161e3b473c60d0eaddb91931
https://doi.org/10.1021/jacs.0c10925

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A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis

Autor: Yun Ji Park, Richard J. Jodts, Jeffrey W. Slater, Reyvin M. Reyes, Valerie J. Winton, Rana A. Montaser, Paul M. Thomas, William B. Dowdle, Anahi Ruiz, Neil L. Kelleher, J. Martin Bollinger, Carsten Krebs, Brian M. Hoffman, Amy C. Rosenzweig

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 119(13)

Significance Methanobactins (Mbns), copper-binding peptidic compounds produced by some bacteria, are candidate therapeutics for human diseases of copper overload. The paired oxazolone-thioamide bidentate ligands of methanobactins are generated from c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf8e01e69ca3a88d50b092392f789ec1
https://pubmed.ncbi.nlm.nih.gov/35320042

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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

Autor: Roman Davydov, Austin E. Herzog, Richard J. Jodts, Kenneth D. Karlin, Brian M. Hoffman

Publikováno v: J Am Chem Soc

In this report, we investigate the physical and chemical properties of monocopper Cu(I) superoxo and Cu(II) peroxo and hydroperoxo complexes. These are prepared by cryoreduction/annealing of the parent [LCu(I)(O(2))](+) Cu(I) dioxygen adducts with th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4e2ce5f08b7267ddf6ff5d9765f2ac0
https://europepmc.org/articles/PMC8785356/

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Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the Cu

Autor: Richard J, Jodts, Matthew O, Ross, Christopher W, Koo, Peter E, Doan, Amy C, Rosenzweig, Brian M, Hoffman

Publikováno v: J Am Chem Soc

In nature, methane is oxidized to methanol by two enzymes, the iron-dependent soluble methane monooxygenase (sMMO) and the copper-dependent particulate MMO (pMMO). While sMMO’s diiron metal active site is spectroscopically and structurally well-cha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::70023b5ffe6d112070fb5a76750b621f
https://pubmed.ncbi.nlm.nih.gov/34498465

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Spectroscopic and Computational Comparisons of Thiolate-Ligated Ferric Nonheme Complexes to Cysteine Dioxygenase: Second-Sphere Effects on Substrate (Analogue) Positioning

Autor: Danushka M. Ekanayake, Sergey V. Lindeman, Thomas C. Brunold, Anne A. Fischer, Richard J Jodts, Joshua R Miller, Adam T. Fiedler

Publikováno v: Inorg Chem

Parallel spectroscopic and computational studies of iron(III) cysteine dioxygenase (CDO) and synthetic models are presented. The synthetic complexes utilize the ligand tris(4,5-diphenyl-1-methylimidazol-2-yl)phosphine ((Ph2)TIP), which mimics the fac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39dbdfa0cc513e54eb262c7474728b69
https://doi.org/10.1021/acs.inorgchem.9b02432

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The Elusive 5′-Deoxyadenosyl Radical: Captured and Characterized by Electron Paramagnetic Resonance and Electron Nuclear Double Resonance Spectroscopies

Autor: William E. Broderick, Joan B. Broderick, Kenichi Yokoyama, Hao Yang, Elizabeth C. McDaniel, Richard J. Jodts, Brian M. Hoffman, Stella Impano, Amanda S. Byer

Publikováno v: Journal of the American Chemical Society. 141:12139-12146

The 5′-deoxyadenosyl radical (5′-dAdo·) abstracts a substrate H atom as the first step in radical-based transformations catalyzed by adenosylcobalamin-dependent and radical S-adenosyl-L-methionine (RS) enzymes. Notwithstanding its central biolog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c9a0003b0c4eec8790df86ba8dcafa8
https://doi.org/10.1021/jacs.9b05926

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