Coordination complexes and biomolecules: A wise wedding for catalysis upgrade

ScienceDirect Publication: Coordination Chemistry Reviews

Publication date:
Source:Coordination Chemistry Reviews
Author(s): Marie Hoarau , Christelle Hureau , Emmanuel Gras , Peter Faller

http://www.sciencedirect.com/science/article/pii/S0010854515001903

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Abstract:
Artificial metalloenzymes, with their high selectivity and specificity combined with a wide scope of reactivity and substrates, constitute an original approach for catalyst development. Different strategies have been proposed for their elaboration, proceeding from modification of natural enzymes using bioengineering methods to de novo protein design. Another bio-inspired methodology for the development of hybrid catalysts consists in the incorporation of coordination complexes into biomolecules, with the aim to upgrade their catalytic abilities. In these systems, the reaction performed by the naked catalyst is modulated by the well-defined structure of the host biomolecule. This conveys added value to the catalyst, such as enantioselectivity or chemoselectivity. DNA, apo-enzymes, proteins and peptides have been engaged in this approach, affording a wide diversity of reactivities and substrates. The resulting systems can then be improved by combined chemical and bioengineering optimization, allowing access to powerful catalysts. Because this approach can virtually be applied to any biomolecule or coordination complex, the elaboration of bio-based hybrid catalysts seems promising for advance in catalysis.

Electrochemical evidence that pyranopterin redox chemistry controls the catalysis of YedY, a mononuclear Mo enzyme

Hope Adamson a, Alexandr N. Simonov b, Michelina Kierzek c, Richard A. Rothery c, Joel H. Weiner c, Alan M. Bond b, and Alison Parkin a,1 a Department of Chemistry, University of York, Heslington, York YO10 5DD, United Kingdom; b School of Chemistry, Monash University, Clayton, VIC 3800, Australia; and c Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA, and approved October 13, 2015 (received for review August 25, 2015) http://www.pnas.org/content/112/47/14506.short A long-standing contradiction in the field of mononuclear Mo enzyme research is that small-molecule chemistry on active-site mimic compounds predicts ligand participation in the electron transfer reactions, but biochemical measurements only suggest metal-centered catalytic electron transfer.With the simultaneous measurement of substrate turnover and reversible electron transfer that is provided by Fourier-...

Tuning Reactivity and Selectivity in Hydrogen Atom Transfer from Aliphatic C–H Bonds to Alkoxyl Radicals: Role of Structural and Medium Effects

Michela Salamone and Massimo Bietti* Dipartimento di Scienze e Tecnologie Chimiche, Università “Tor Vergata”, Via della Ricerca Scientifica, Italy Acc. Chem. Res., Article ASAP DOI: 10.1021/acs.accounts.5b00348 Publication Date (Web): November 6, 2015 クメンパーオキシドを光で開裂させることにより、生成するクミルアルコキシルラジカルによるアルカンやアミンのC–H切断の速度定数などの情報がまとまっています。溶媒や、酸、基質の形が反応速度定数に与える影響を定量的に評価しています。酸化反応をしている方は、手元に置いておいても良いのでしょうか。

Rhenium(V)–oxo corrolazines: isolating redox-active ligand reactivity

Jan Paulo T. Zaragoza,a Maxime A. Sieglera and David P. Goldberg* Chem. Commun., 2015, Advance Article DOI: 10.1039/C5CC07956J Received 22 Sep 2015, Accepted 15 Oct 2015 First published online 28 Oct 2015 http://pubs.rsc.org/en/content/articlelanding/2015/cc/c5cc07956j#!divAbstract Abstract The synthesis of the first example of a third-row metallocorrolazine characterized by single crystal X-ray diffraction is reported. This ReV(O) porphyrinoid complex shows an exclusively ligand-based reactivity with strong acids and oxidizing agents. The one-electron oxidized π-radical-cation complex is capable of H-atom abstraction.

C–H Bond Oxidation Catalyzed by an Imine-Based Iron Complex: A Mechanistic Insight

Giorgio Olivo§¶, Martina Nardi§, Diego Vìdal¶, Alessia Barbieri§, Andrea Lapi§‡, Laura Gómez¶⊥, Osvaldo Lanzalunga§‡, Miquel Costas*¶, and Stefano Di Stefano*§‡ § Università degli Studi di Roma, Rome, Italy ¶ Institut de Química Computacional i Catàlisi (IQCC), Girona, Spain Inorg. Chem., 2015, 54 (21), pp 10141–10152 DOI: 10.1021/acs.inorgchem.5b01500 Publication Date (Web): October 12, 2015 A family of imine-based nonheme iron(II) complexes (LX)2Fe(OTf)2 has been prepared, characterized, and employed as C–H oxidation catalysts. Ligands LX (X = 1, 2, 3, and 4) stand for tridentate imine ligands resulting from spontaneous condensation of 2-pycolyl-amine and 4-substituted-2-picolyl aldehydes. Fast and quantitative formation of the complex occurs just upon mixing aldehyde, amine, and Fe(OTf)2 in a 2:2:1 ratio in acetonitrile solution. The solid-state structures of (L1)2Fe(OTf)(ClO4) and (L3)2Fe(OTf)2 are reported, showing a low-spin octahedral iron center, with the lig...

Oxidative Alkene Cleavage Catalysed by Manganese-Dependent Cupin TM1459 from Thermotoga maritima

van Hajnal 1 , Kurt Faber 1,2 , Helmut Schwab 1,3 , Mélanie Hall 2,* and Kerstin Steiner 1,* a acib, Austrian Centre of Industrial Biotechnology GmbH, Petersgasse 14, 8010 Graz, Austria Fax: ( + 43)-316-873-9302; phone: ( + 43)-316-873-9346; e-mail: kerstin.steiner@acib.at b Department of Chemistry, University of Graz, Heinrichstraße 28, 8010 Graz, Austria Fax: ( + 43)-316-380-9840; phone: ( + 43)-316-380-5479; e-mail: melanie.hall@uni-graz.at c Institute of Molecular Biotechnology, TU Graz, Petersgasse 14, 8010 Graz, Austria Adv .S ynth. Catal. 2015 , 357 , 3 309 –3 316 DOI: 10.1002/adsc.201500608 Abstract A novel biocatalytic oxidative alkene cleavage activity was identified in protein TM1459 from Thermotoga maritima , a so far uncharacterised metalloprotein with a cupin fold, which preferentially binds manganese (over iron and zinc). Various styrene derivat...

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