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Selective Alcohol Oxidation by a Copper-TEMPO Catalyst: Mechanistic Insights by Simultaneously Coupled Operando EPR/UV-Vis/ATR-IR Spectroscopy

Dr. Jabor Rabeah 1,* , Dr. Ursula Bentrup 1,* , Prof. Dr. Reinhard Stößer 2 and Prof. Dr. Angelika Brückner 1,* 1 .Leibniz-Institut für Katalyse e.V. an der Universität Rostock, Albert-Einstein-Str. 29a, 18059 Rostock (Germany)   2 .Institut für Chemie-Humboldt-Universität zu Berlin, Brook-Taylor-Str. 2, 12489 Berlin-Adlershof (Germany) Article first published online: 14 JUL 2015 DOI: 10.1002/anie.201504813 Abstract The first coupled operando EPR/UV-Vis/ATR-IR spectroscopy setup for mechanistic studies of gas-liquid phase reactions is presented and exemplarily applied to the well-known copper/TEMPO-catalyzed (TEMPO=(2,2,6,6-tetramethylpiperidin-1-yl)oxyl) oxidation of benzyl alcohol. In contrast to previous proposals, no direct redox reaction between TEMPO and Cu I /Cu II has been detected. Instead, the role of TEMPO is postulated to be the stabilization of a (bpy)(NMI)Cu II -O 2 ⋅− -TEMPO (bpy=2,2′-bipyridine, NMI= N -methylimidazole) intermedia...

Bioinduced Room-Temperature Methanol Reforming

M.Sc. Leo E. Heim 1 , Dipl.-Chem. Daniel Thiel 1 , Christian Gedig 1 , Priv.-Doz. Dr. Jan Deska 1,2,* andPriv.-Doz. Dr. Martin H. G. Prechtl 1,* 1 .Department Chemie, Universität zu Köln, Greinstrasse 4-6, 50939 Cologne (Germany) 2 .Current address: Department of Chemistry, Aalto University, Kemistintie 1, 00076 Espoo (Finland) Article first published online: 14 JUL 2015 DOI: 10.1002/anie.201503737 Abstract Imitating nature′s approach in nucleophile-activated formaldehyde dehydrogenation, air-stable ruthenium complexes proved to be exquisite catalysts for the dehydrogenation of formaldehyde hydrate as well as for the transfer hydrogenation to unsaturated organic substrates at loadings as low as 0.5 mol %. Concatenation of the chemical hydrogen-fixation route with an oxidase-mediated activation of methanol gives an artificial methylotrophic in vitro metabolism providing methanol-derived reduction equivalents for synthetic hydrogenation purposes. Moreover,...

Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins

Rae Ana Snyder † , Justine Betzu ‡ , Susan E. Butch ‡ , Amanda J. Reig * ‡ , William F. DeGrado * § , and Edward I. Solomon * † ∥ † Department of Chemistry, Stanford University , Stanford, California 94305, United States ‡ Department of Chemistry, Ursinus College , Collegeville, Pennsylvania 19426, United States § Department of Pharmaceutical Chemistry, University of California San Francisco , San Francisco, California 94143, United States ∥ Stanford Synchrotron Radiation Laboratory, Stanford University, SLAC , Menlo Park, California 94025, United States Biochemistry , Article ASAP DOI: 10.1021/acs.biochem.5b00324 Publication Date (Web): July 8, 2015 Copyright © 2015 American Chemical Society *E-mail: areig@ursinus.edu . Phone: (610) 409-3383 ., *E-mail: Bill.DeGrado@ucsf.edu . Phone: (415) 476-9679 ., *E-mail: edward.solomon@stanford.edu . Phone: (650) 723-9104 . Abstract DFsc (single-chain due ferri ) proteins allow for modeling binuclear non...

Molecular-Level Insight into the Differential Oxidase and Oxygenase Reactivities of de Novo Due Ferri Proteins

Rae Ana Snyder † , Susan E. Butch ‡ , Amanda J. Reig * ‡ , William F. DeGrado * ⊥ , and Edward I. Solomon * † § † Department of Chemistry, Stanford University , Stanford, California 94305, United States , ‡ Department of Chemistry, Ursinus College , Collegeville, Pennsylvania 19426, United States , ⊥ Department of Pharmaceutical Chemistry, University of California , San Francisco, California 94143, United States § Stanford Synchrotron Radiation Laboratory, SLAC, Stanford University , Menlo Park, California 94025, United States J. Am. Chem. Soc. , Article ASAP DOI: 10.1021/jacs.5b03524 Publication Date (Web): June 19, 2015 Copyright © 2015 American Chemical Society http://pubs.acs.org/doi/pdf/10.1021/jacs.5b03524 Abstract Using the single-chain due ferri (DFsc) peptide scaffold, the differential oxidase and oxygenase reactivities of two 4A→4G variants, one with two histidines at the diiron center (G4DFsc) and the other with three histidin...