High-valent intermediates of heme proteins and model compounds.

Recent computational and experimental probes of high-valent intermediates in heme proteins and model compounds reveal a rich spectrum of chemical behavior that is dependent on the nature of the proximal ligand, metal center, distal- and proximal-binding site environment, porphyrin macrocycle architecture, and consequent electronic structure. The results of such studies reveal an underlying complexity, which is simply understood once one is cognizant of the 'chameleon'-like behavior of such intermediates is determined by the high-valent intermediate environment.

[1]  Gilda H. Loew,et al.  Structure and Spectra of Ferrous Dioxygen and Reduced Ferrous Dioxygen Model Cytochrome P450 , 1998 .

[2]  M. Newcomb,et al.  Hypersensitive radical probe studies of chloroperoxidase-catalyzed hydroxylation reactions. , 1998, Chemical research in toxicology.

[3]  Sason Shaik,et al.  Medium Polarization and Hydrogen Bonding Effects on Compound I of Cytochrome P450: What Kind of a Radical Is It Really? , 2000 .

[4]  L. Hager,et al.  Unusual propargylic oxidations catalyzed by chloroperoxidase. , 1998, Biochemical and biophysical research communications.

[5]  Abhik Ghosh,et al.  A First-Principles Quantum Chemical Analysis of the Factors Controlling Ruffling Deformations of Porphyrins: Insights from the Molecular Structures and Potential Energy Surfaces of Silicon, Phosphorus, Germanium, and Arsenic Porphyrins and of a Peroxidase Compound I Model , 1999 .

[6]  E. Allain,et al.  Highly Enantioselective Epoxidation of Disubstituted Alkenes with Hydrogen Peroxide Catalyzed by Chloroperoxidase. , 1993 .

[7]  B. Malmstrom.  Enzymology of Oxygen , 1982 .

[8]  W. Woggon,et al.  Cytochrome P450: Significance, reaction mechanisms and active site analogues , 1996 .

[9]  S. Adachi,et al.  Spectroscopic and Kinetic Studies on Reaction of Cytochrome P450nor with Nitric Oxide , 1995, The Journal of Biological Chemistry.

[10]  Robert J. Deeth.  Saddle Distortions of Ferryl-Porphyrin Models for Peroxidase Compound I: A Density Functional Study , 1999 .

[11]  Abhik Ghosh,et al.  Electrochemical and Electronic Absorption Spectroscopic Studies of Substituent Effects in Iron(IV) and Manganese(IV) Corroles. Do the Compounds Feature High-Valent Metal Centers or Noninnocent Corrole Ligands? Implications for Peroxidase Compound I and II Intermediates , 2001 .

[12]  Sason Shaik,et al.  The High-Valent Compound of Cytochrome P450: The Nature of the Fe-S Bond and the Role of the Thiolate Ligand as an Internal Electron Donor. , 2001, Angewandte Chemie.

[13]  Edward I. Solomon,et al.  Inorganic electronic structure and spectroscopy , 1999 .

[14]  J Berendzen,et al.  The catalytic pathway of cytochrome p450cam at atomic resolution. , 2000, Science.

[15]  M. Grodzicki,et al.  LOCAL DENSITY FUNCTIONAL STUDY OF OXOIRON(IV) PORPHYRIN COMPLEXES AND THEIR ONE-ELECTRON OXIDIZED DERIVATIVES. AXIAL LIGAND EFFECTS , 1997 .

[16]  Sason Shaik,et al.  The Experimentally Elusive Oxidant of Cytochrome P450: A Theoretical “Trapping” Defining More Closely the “Real” Species , 2001, Chembiochem : a European journal of chemical biology.

[17]  D. Case,et al.  Density Functional Study on the Electronic Structures of Model Peroxidase Compounds I and II , 1997 .

[18]  D. Gamelin,et al.  [5] Bioinorganic spectroscopy , 1995 .

[19]  Gilda H. Loew,et al.  Proximal ligand effects on electronic structure and spectra of compound I of peroxidases , 2001 .

[20]  X Wang,et al.  Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[21]  M T Green,et al.  The structure and spin coupling of catalase compound I: a study of noncovalent effects. , 2001, Journal of the American Chemical Society.

[22]  L. Waskell,et al.  Calculation of the electronic structure and spectra of model cytochrome P450 compound I. , 2001, Journal of inorganic biochemistry.

[23]  Louis Noodleman,et al.  Valence bond description of antiferromagnetic coupling in transition metal dimers , 1981 .

[24]  Gilda H. Loew,et al.  THEORETICAL INVESTIGATION OF THE PROTON ASSISTED PATHWAY TO FORMATION OF CYTOCHROME P450 COMPOUND I , 1998 .

[25]  J. Tainer,et al.  Structure of nitric oxide synthase oxygenase dimer with pterin and substrate. , 1998, Science.

[26]  N. Bec,et al.  Reaction of Neuronal Nitric-oxide Synthase with Oxygen at Low Temperature , 1998, The Journal of Biological Chemistry.

[27]  A. Blomberg,et al.  Reaction Mechanism of Compound I Formation in Heme Peroxidases: A Density Functional Theory Study , 1999 .

[28]  D. Dodds,et al.  Chloroperoxidase-catalyzed asymmetric oxidations: substrate specificity and mechanistic study. , 1995 .

[29]  Michael T. Green.  Imidazole-Ligated Compound I Intermediates: The Effects of Hydrogen Bonding , 2000 .

[30]  S. Shaik,et al.  What is the difference between the manganese porphyrin and corrole analogues of cytochrome P450's compound I? , 2001, Chemistry.

[31]  S. Shaik,et al.  A theoretical study of electronic factors affecting hydroxylation by model ferryl complexes of cytochrome P-450 and horseradish peroxidase , 1999 .

[32]  K. Hatano,et al.  Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor. , 1993, The Journal of biological chemistry.

[33]  J. Dawson,et al.  Heme-Containing Oxygenases. , 1996, Chemical reviews.

[34]  H. Wagenknecht,et al.  Identification of intermediates in the catalytic cycle of chloroperoxidase. , 1997, Chemistry & biology.

[35]  S. Shaik,et al.  Chameleon States: High-Valent Metal-Oxo Species of Cytochrome P450 and Its Ruthenium Analogue. , 2001, Angewandte Chemie.

[36]  Z. Gross.  High-valent corrole metal complexes , 2001, JBIC Journal of Biological Inorganic Chemistry.

[37]  O. Hayaishi.  Molecular mechanisms of oxygen activation , 1974 .

[38]  G. Loew,et al.  Investigation of the proton-assisted pathway to formation of the catalytically active, ferryl species of P450s by molecular dynamics studies of P450eryF. , 1996, Journal of the American Chemical Society.

[39]  S. Colonna,et al.  Enantioselective oxidations of sulfides catalyzed by chloroperoxidase. , 1990, Biochemistry.

[40]  Abhik Ghosh,et al.  High-valent transition metal centers and noninnocent ligands in metalloporphyrins and related molecules: a broad overview based on quantum chemical calculations , 2001, JBIC Journal of Biological Inorganic Chemistry.

[41]  Michael T. Green.  Evidence for Sulfur-Based Radicals in Thiolate Compound I Intermediates , 1999 .