Oxygen Atom Transfer Using an Iron(IV)-Oxo Embedded in a Tetracyclic N-Heterocyclic Carbene System: How Does the Reactivity Compare to Cytochrome P450 Compound I?
作者： Fabián G. Cantú Reinhard , Sam P. de Visser
关键词: Reactivity (chemistry) 、 Transition metal 、 Molecular orbital 、 Chemistry 、 Carbene 、 Photochemistry 、 Ligand 、 Valence bond theory 、 Catalysis 、 Hydroxylation 、 Medicinal chemistry
摘要: N-Heterocyclic carbenes (NHC) are commonly featured as ligands in transition metal catalysis. Recently, a cyclic system containing four NHC groups with central iron atom was synthesized and its iron(IV)-oxo species, [FeIV (O)(cNHC4 )]2+ , characterized. This tetracyclic ligand may give the species unique catalytic properties compared to traditional non-heme heme systems. Therefore, we performed computational study on structure reactivity of complex substrate hydroxylation epoxidation reactions. The patterns cytochrome P450 Compound I models it is shown that an effective oxidant oxidative power analogous Compound I. Unfortunately, polar solvents, solvent molecule will bind sixth position decrease activity oxidant. A molecular orbital valence bond analysis provides insight into origin differences makes predictions how further exploit these systems chemical
manchester.ac.uk参考文章(97)
Heather M. Neu, Regina A. Baglia, David P. Goldberg, A Balancing Act: Stability versus Reactivity of Mn(O) Complexes. Accounts of Chemical Research. ,vol. 48, pp. 2754- 2764 ,(2015) , 10.1021/ACS.ACCOUNTS.5B00273
Peter Nicholls, Ignacio Fita, Peter C. Loewen, Enzymology and structure of catalases Advances in Inorganic Chemistry. ,vol. 51, pp. 51- 106 ,(2000) , 10.1016/S0898-8838(00)51001-0
D.B. Goodin, D.E. Mcree, The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme. Biochemistry. ,vol. 32, pp. 3313- 3324 ,(1993) , 10.2210/PDB1CCA/PDB
David Balcells, Christophe Raynaud, Robert H. Crabtree, Odile Eisenstein, A Rational Basis for the Axial Ligand Effect in C−H Oxidation by [MnO(porphyrin)(X)]+ (X = H2O, OH−, O2−) from a DFT Study Inorganic Chemistry. ,vol. 47, pp. 10090- 10099 ,(2008) , 10.1021/IC8013706
Miquel Costas, Mark P. Mehn, Michael P. Jensen, Lawrence Que, Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates Chemical Reviews. ,vol. 104, pp. 939- 986 ,(2004) , 10.1021/CR020628N
J. T. Groves, The bioinorganic chemistry of iron in oxygenases and supramolecular assemblies Proceedings of the National Academy of Sciences of the United States of America. ,vol. 100, pp. 3569- 3574 ,(2003) , 10.1073/PNAS.0830019100
J. Rittle, M. T. Green, Cytochrome P450 Compound I: Capture, Characterization, and C-H Bond Activation Kinetics Science. ,vol. 330, pp. 933- 937 ,(2010) , 10.1126/SCIENCE.1193478
Suresh Kumar, Abayomi S. Faponle, Prasenjit Barman, Anil Kumar Vardhaman, Chivukula V. Sastri, Devesh Kumar, Sam P. de Visser, Long-Range Electron Transfer Triggers Mechanistic Differences between Iron(IV)-Oxo and Iron(IV)-Imido Oxidants Journal of the American Chemical Society. ,vol. 136, pp. 17102- 17115 ,(2014) , 10.1021/JA508403W
Masanori Sono, Mark P. Roach, Eric D. Coulter, John H. Dawson, Heme-Containing Oxygenases Chemical Reviews. ,vol. 96, pp. 2841- 2888 ,(1996) , 10.1021/CR9500500
Paul R. Ortiz de Montellano, Hydrocarbon hydroxylation by cytochrome P450 enzymes. Chemical Reviews. ,vol. 110, pp. 932- 948 ,(2010) , 10.1021/CR9002193