Resonance Raman spectra of highly oxidized metalloporphyrins and heme proteins
暂无分享,去创建一个
[1] Y. Mizutani,et al. Resonance Raman Characterization of Iron(III) Porphyrin N-Oxide: Evidence for an Fe-O-N Bridged Structure , 1994 .
[2] S. Yoshikawa,et al. Time-resolved resonance Raman elucidation of the pathway for dioxygen reduction by cytochrome c oxidase , 1993 .
[3] H. Fujii. Effects of the electron-withdrawing power of substituents on the electronic structure and reactivity in oxoiron(IV) porphyrin π-cation radical complexes , 1993 .
[4] I. Morishima,et al. Preparation, characterization, and reaction of novel dioxoruthenium(VI) porphyrin cation radical complexes , 1993 .
[5] T. Egawa,et al. Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase. , 1993, Biochemistry.
[6] T. Egawa,et al. Observation of the FeIV=O stretching Raman band for a thiolate‐ligated heme protein Compound I of chloroperoxidase , 1992, FEBS letters.
[7] H. V. Van Wart,et al. Resonance Raman spectra of horseradish peroxidase and bovine liver catalase compound I species. Evidence for predominant 2A2u pi-cation radical ground state configurations. , 1992, The Journal of biological chemistry.
[8] H. Fujii,et al. Preparation and characterization of an A1u (Oxo) iron(IV) porphyrin .pi.-cation-radical complex , 1992 .
[9] R. Gennis,et al. Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy. , 1991, Biochemistry.
[10] Y. Nishimura,et al. Imidazole adducts of (octaethylporphinato) iron(III) methoxide: resonance Raman evidence for the formation of hydrogen bonds between sterically hindered imidazoles and methoxide , 1991 .
[11] S. Yoshikawa,et al. Time-Resolved Resonance Raman Investigation of Cytochrome Oxidase Catalysis: Observation of a New Oxygen-Isotope Sensitive Raman Band , 1991 .
[12] K. Aoyagi,et al. Resonance Raman Study on Phot on eduction of Iron–Porphyrins. A Novel Insight into the Ligand-Aided Process , 1991 .
[13] Y. Mizutani,et al. Resonance Raman characterization of ferric and ferryl porphyrin .pi. cation radicals and the FeIV:0 stretching frequency , 1991 .
[14] T. Egawa,et al. Observation of the O-O stretching Raman band for cytochrome P-450cam under catalytic conditions. , 1991, The Journal of biological chemistry.
[15] K. Nakamoto,et al. Resonance Raman spectra of two isomeric dioxygen adducts of iron(II) porphyrins and .pi.-cation radical and nonradical oxoferryl porphyrins produced in dioxygen matrixes: simultaneous observation of more than seven oxygen isotope sensitive bands , 1991 .
[16] D. Rousseau,et al. Ferryl and hydroxy intermediates in the reaction of oxygen with reduced cytochrome c oxidase , 1990, Nature.
[17] Y. Mizutani,et al. Resonance Raman pursuit of the change from iron(II)-oxygen (FeII-O2) to iron(III)-hydrohxyl (FeIII-OH) via iron(IV):oxygen (FeIV:O) in the autoxidation of ferrous iron-porphyrin , 1990 .
[18] S. Takahashi,et al. Observation of the Fe4+ = O stretching Raman band for cytochrome oxidase compound B at ambient temperature. , 1990, The Journal of biological chemistry.
[19] G. Babcock,et al. Appearance of the v(FeIV = O) vibration from a ferryl-oxo intermediate in the cytochrome oxidase/dioxygen reaction. , 1990, Biochemistry.
[20] G. Babcock,et al. Factors affecting the iron-oxygen vibrations of ferrous oxy and ferryl oxo heme proteins and model compounds , 1990 .
[21] Y. Ozaki,et al. Alcohol-catalyzed photoreduction of iron-porphyrin complexes revealed by resonance raman and absorption spectroscopies , 1990 .
[22] R. Czernuszewicz,et al. Influence of porphyrin radical type on vanadium-oxygen double bond strength in vanadyl porphyrin cation radicals: implications for heme protein intermediates , 1990 .
[23] S. Strauss,et al. Influence of symmetry on the vibrational spectra of Zn(TPP), Zn(TPC), and Zn(TPiBC) , 1990 .
[24] K. Nakamoto,et al. Resonance Raman spectra of reaction intermediates in the oxidation process of ruthenium(II) and iron(II) porphyrins , 1990 .
[25] Xiaoyuan Li,et al. Metalloporphyrin structure and dynamics from resonance raman spectroscopy , 1990 .
[26] Xiaoyuan Li,et al. Consistent porphyrin force field. 2. Nickel octaethylporphyrin skeletal and substituent mode assignments from nitrogen-15, meso-d4, and methylene-d16 Raman and infrared isotope shifts , 1990 .
[27] Catherine M. Reczek,et al. Resonance Raman characterization of heme Fe(IV)=O groups of intermediates of yeast cytochrome C peroxidase and lactoperoxidase , 1989 .
[28] V. Palaniappan,et al. Resonance Raman spectroscopy of horseradish peroxidase derivatives and intermediates with excitation in the near ultraviolet. , 1989, The Journal of biological chemistry.
[29] H. V. Van Wart,et al. Resonance Raman spectra of bovine liver catalase compound II. Similarity of the heme environment to horseradish peroxidase compound II. , 1989, The Journal of biological chemistry.
[30] D B Goodin,et al. Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. , 1989, Science.
[31] G. Babcock,et al. An ENDOR study of spin distributions in octaethylmetalloporphyrin .pi. cation radicals , 1989 .
[32] C. Reed,et al. Metalloporphyrin .pi.-cation radicals: intrinsically ruffled or planar core conformations? Molecular structure mesitylporphinatocopper(II) hexachloroantimonate , 1989 .
[33] K. Paeng,et al. The resonance Raman spectrum of a ferrylporphyrin cation radical and its photodegradation in the presence of methanol , 1989 .
[34] Xiaoyuan Li,et al. Resonance Raman spectroscopy reveals a1u vs. a2u character and pseudo-Jahn-Teller distortion in radical cations of nickel(II), copper(II), and chloroiron(III) octaethyl- and tetraphenylporphyrins , 1989 .
[35] Paul M. Champion,et al. Elementary electronic excitations and the mechanism of cytochrome P450 , 1989 .
[36] K. Nakamoto,et al. Resonance raman spectra of nitridoiron(V) porphyrin intermediates produced by laser photolysis , 1989 .
[37] G. Babcock,et al. Resonance Raman vibrational analysis of Cu sup II , Fe sup III , and Co sup III porphyrin. pi. cation radicals and their meso-deuteriated analogues , 1989 .
[38] R. Czernuszewicz,et al. A low‐temperature bulk electrolysis cell for in situ resonance Raman spectroelectrochemistry: Observation of the FeIVO stretching frequency for electrogenerated ferryl tetramesitylporphyrin , 1988 .
[39] K. Paeng,et al. The resonance Raman spectrum of horseradish peroxidase compound I , 1988 .
[40] A. Gold,et al. Oxoferryl complexes of the halogenated (porphinato)iron catalyst [tetrakis(2,6-dichlorophenyl)porphinato]iron , 1988 .
[41] T. Kitagawa,et al. Novel optical device for simultaneous measurements of Raman and absorption spectra: Application to photolabile reaction intermediates of hemeproteins , 1988 .
[42] R. Wever,et al. Identification and properties of an oxoferryl structure in myeloperoxidase compound II. , 1988, Biochemistry.
[43] R. Czernuszewicz,et al. Effects of solvents, axial ligation, and radical cation formation on the V=O stretching Raman frequency in vanadyl porphyrins: implications for peroxidase intermediates , 1988 .
[44] K. Nakamoto,et al. Formation of nitridoiron(V) porphyrins detected by resonance Raman spectroscopy , 1988 .
[45] G. Babcock,et al. Time-resolved and static resonance Raman spectroscopy of horseradish peroxidase intermediates. , 1988, Biochemistry.
[46] V. Thanabal,et al. Proton NMR characterization of the catalytically relevant proximal and distal hydrogen-bonding networks in ligated resting state horseradish peroxidase , 1988 .
[47] K. Nakamoto,et al. Detection of the Fe-O-O-Fe intermediate in the oxidation reaction of ferrous porphyrins by resonance Raman spectroscopy , 1988 .
[48] T. Kitagawa,et al. Observation of the FeIV=O stretching Raman band for a ferryl porphyrin .pi. cation radical , 1987 .
[49] G. Babcock,et al. Iron porphyrin .pi. cation radicals: solution resonance Raman spectra of iron octaethylporphyrinates, (OEP.bul.+)FeIII(X)(X') , 1987 .
[50] G. E. Leroi,et al. Vibrational, electronic, and structural properties of cobalt, copper, and zinc octaethylporphyrin .pi. cation radicals , 1987 .
[51] H. Hori,et al. Influence of heme-surrounding amino acid residues on the manganese (V)-nitrido bond in manganese-substituted hemoproteins: resonance Raman evidence for porphyrin core expansion and reduction of the manganese(V)-nitrido stretching force constant. , 1987, Biochemistry.
[52] G. Babcock,et al. Resonance Raman spectroscopic detection of demetallation of metalloporphyrin .pi. cation radicals , 1987 .
[53] T. Kitagawa,et al. Device for simultaneous measurements of transient Raman and absorption spectra of enzymic reactions: application to compound I of horseradish peroxidase , 1987 .
[54] G. G. Deanin,et al. Heme-linked ionizations of myeloperoxidase detected by Raman difference spectroscopy. A comparison with plant and yeast peroxidases. , 1987, Biophysical journal.
[55] G. Babcock,et al. Characterization of six-coordinate ferryl protoheme by resonance Raman and optical absorption spectroscopy , 1987 .
[56] K. A. Joergensen. The mechanism of stereoselective epoxidation of alkenes by oxo-iron porphyrins , 1987 .
[57] I. Yamazaki,et al. Oxygen exchange between the Fe(IV)O heme and bulk water for the A2 isozyme of horseradish peroxidase , 1986, FEBS letters.
[58] J. Groves,et al. Preparation and characterization of an iron(III) porphyrin N-oxide. , 1986, Journal of the American Chemical Society.
[59] G. Babcock,et al. One-electron oxidation of the porphyrin ring of cobaltous octaethylporphyrin (CoIIOEP). Absorption and resonance Raman spectral characteristics of the CoIIOEP+.cntdot.ClO4- .pi.-cation radical , 1986 .
[60] T. Inubushi,et al. Resonance Raman study on cytochrome c peroxidase and its intermediate. Presence of the Fe(IV) = O bond in compound ES and heme-linked ionization. , 1986, The Journal of biological chemistry.
[61] Dongho Kim,et al. Resonance Raman spectra of metallooctaethylporphyrin cation radicals with a1u and a2u orbital character , 1986 .
[62] P. Champion,et al. Resonance Raman studies of isotopically labeled chloroperoxidase. , 1986, Biochemistry.
[63] T. Kitagawa,et al. Resonance Raman evidence for oxygen exchange between the FeIV = O heme and bulk water during enzymic catalysis of horseradish peroxidase and its relation with the heme-linked ionization. , 1986, Proceedings of the National Academy of Sciences of the United States of America.
[64] K. Nakamoto,et al. Resonance Raman spectra of ferrylporphyrins and related compounds in dioxygen matrices , 1986 .
[65] H. Goff,et al. Solution characterization of copper(II) and silver(II) porphyrins and the one-electron oxidation products by nuclear magnetic resonance spectroscopy. , 1986, Journal of the American Chemical Society.
[66] P. Gans,et al. High-valent iron porphyrins: synthesis, x-ray structures, .pi.-cation radical formulation, and notable magnetic properties of chloro(meso-tetraphenylporphinato)iron(III) hexachloroantimonate and bis(perchlorato)(meso-tetraphenylporphinato)iron(III) , 1986 .
[67] J. Dawson,et al. Ligand and halide binding properties of chloroperoxidase: peroxidase-type active site heme environment with cytochrome P-450 type endogenous axial ligand and spectroscopic properties. , 1986, Biochemistry.
[68] B C Finzel,et al. The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. , 1985, The Journal of biological chemistry.
[69] A. Balch,et al. A complex containing a nickel-oxygen unit at the center of a porphyrin. The x-ray crystal and molecular structure of the nickel(II) complex of octaethylporphyrin N-oxide dianion , 1985 .
[70] S. Gellman,et al. Functionalized nitrogen atom transfer catalyzed by cytochrome P-450 , 1985 .
[71] G. Babcock,et al. Resonance Raman scattering from horseradish peroxidase compound I , 1985 .
[72] M. Rossmann,et al. The active center of catalase. , 1985, Journal of molecular biology.
[73] D. F. Bocian,et al. Resonance Raman spectra of chromium(V) and manganese(V) porphyrin nitrides , 1985 .
[74] Catherine M. Reczek,et al. Heme-linked ionization of horseradish peroxidase compound II monitored by the resonance Raman Fe(IV)=O stretching vibration. , 1985, The Journal of biological chemistry.
[75] D. Rousseau,et al. Resonance Raman evidence of chloride binding to the heme iron in myeloperoxidase , 1985, FEBS letters.
[76] H. E. Wart,et al. Resonance Raman studies of the photoreduction of horseradish peroxidase compounds I and II , 1985 .
[77] Catherine M. Reczek,et al. Observation of the FeIVO stretching vibration of ferryl myoglobin by resonance Raman spectroscopy , 1985 .
[78] A. Balch,et al. Structure of octaethylporphyrin N-oxide and the characterization of its nickel(II) and copper(II) complexes , 1985 .
[79] R. Wever,et al. Raman characterization of human leukocyte myeloperoxidase and bovine spleen green haemoprotein. Insight into chromophore structure and evidence that the chromophores of myeloperoxidase are equivalent. , 1985, Biochimica et biophysica acta.
[80] Catherine M. Reczek,et al. Resonance Raman spectroscopic characterizations of horseradish peroxidase. Observations of the FeIV = O stretching vibration of Compound II , 1985 .
[81] I. Morishima,et al. Nuclear magnetic resonance studies of metalloporphyrin .pi.-cation radicals as models for compound I of peroxidases , 1984 .
[82] T. Poulos,et al. X-ray absorption studies of intermediates in peroxidase activity. , 1984, Archives of biochemistry and biophysics.
[83] A. Balch,et al. Oxygenation patterns for iron(II) porphyrins. Peroxo and ferryl (FeIVO) intermediates detected by proton nuclear magnetic resonance spectroscopy during the oxygenation of (tetramesitylporphyrin)iron(II) , 1984 .
[84] D. Rousseau,et al. Confirmation of the assignment of the iron-histidine stretching mode in myoglobin , 1984 .
[85] S. S. Sibbett,et al. Structural analysis of myeloperoxidase by resonance Raman spectroscopy. , 1984, Biochemistry.
[86] J. Terner,et al. Resonance Raman scattering from hyperporphyrin absorption bands of molybdenum tetraphenylporphyrin , 1984 .
[87] K. Nakamoto,et al. Formation of ferryltetraphenylporphyrin by laser irradiation , 1984 .
[88] S. Yoshikawa,et al. Iron-histidine stretching Raman lines of the aa3-type cytochrome oxidases , 1983 .
[89] M. Hendrich,et al. Chemical nature of the porphyrin pi cation radical in horseradish peroxidase compound I. , 1983, Biochemistry.
[90] S. Nakamura,et al. Distinct heme-substrate interactions of lactoperoxidase probed by resonance Raman spectroscopy: difference between animal and plant peroxidases. , 1983, Biochemistry.
[91] K. Gersonde,et al. METAL COMPLEXES WITH TETRAPYRROLE LIGANDS. 29. SYNTHESIS AND ELECTRON SPIN RESONANCE SPECTRA AND ELECTRON NUCLEAR DOUBLE RESONANCE INVESTIGATIONS OF NITRIDOCHROMIUM(V) PORPHYRINS , 1983 .
[92] J. Groves,et al. Synthesis and molecular structure of a nitrido(porphyrinato)chromium(V) complex , 1983 .
[93] A. Balch,et al. X-RAY CRYSTALLOGRAPHIC CHARACTERIZATION OF AN IRON PORPHYRIN WITH A VINYLIDENE CARBENE INSERTED INTO AN IRON-NITROGEN BOND , 1982 .
[94] T. Kitagawa,et al. Resonance Raman spectra of the reaction intermediates of horseradish peroxidase catalysis , 1982 .
[95] B. Stallard,et al. Resonance Raman detection of an iron-sulfur bond in cytochrome P 450cam , 1982 .
[96] K. Itoh,et al. RESONANCE RAMAN SCATTERING STUDY ON THE π-CATION RADICALS OF MAGNESIUM, ZINC, AND COPPER TETRAPHENYLPORPHINES , 1982 .
[97] R. Haushalter,et al. Synthesis, Characterization, and Molecular Structure of Oxo(porphyrinato)chromium(IV) Complexes , 1982 .
[98] A. Segal,et al. Studies of cyanide binding to myeloperoxidase by electron paramagnetic resonance and magnetic circular dichroism spectroscopies , 1982 .
[99] R. Hoffmann,et al. Metalloporphyrins with unusual geometries. 2. Slipped and skewed bimetallic structures, carbene and oxo complexes, and insertions into metal-porphyrin bonds , 1981 .
[100] R. Wever,et al. Spectral properties of myeloperoxidase and its ligand complexes. , 1981, Biochimica et biophysica acta.
[101] S. Obara,et al. Ab initio molecular orbital calculation of fe‐porphine with a double zeta basis set , 1981 .
[102] A. Balch,et al. Reversible migration of an axial carbene ligand into an iron-nitrogen bond on a porphyrin. Implications for high oxidation states of heme enzymes and heme catabolism , 1981 .
[103] R. Haushalter,et al. High-valent iron-porphyrin complexes related to peroxidase and cytochrome P-450 , 1981 .
[104] D. Mansuy,et al. An iron(III)-porphyrin complex with a vinylidene group inserted into an iron-nitrogen bond: relevance to the structure of the active oxygen complex of catalase , 1981 .
[105] T. Kitagawa,et al. Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line. , 1981, The Journal of biological chemistry.
[106] L. K. Hanson,et al. Electron pathways in catalase and peroxidase enzymic catalysis. Metal and macrocycle oxidations of iron porphyrins and chlorins , 1981 .
[107] H. Hori,et al. Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin , 1980 .
[108] K. Nagai,et al. Quaternary structures and low frequency molecular vibrations of haems of deoxy and oxyhaemoglobin studied by resonance raman scattering. , 1980, Journal of molecular biology.
[109] K. Nagai,et al. Resonance Raman spectra of myoglobins reconstituted with spirographis and isospirographis hemes and iron 2,4-diformylprotoporphyrin IX. Effect of formyl substitution at the heme periphery. , 1980, Biochemistry.
[110] S. Asher,et al. Resonance Raman examination of axial ligand bonding and spin-state equilibria in metmyoglobin hydroxide and other heme derivatives. , 1979, Biochemistry.
[111] K. Nagai,et al. Assignment of the Fe—Nϵ (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin , 1979 .
[112] N. Yu,et al. A Raman spectroscopic study of the interaction of divalent metal ions with adenine moiety of adenosine 5'-triphosphate. , 1979, The Journal of biological chemistry.
[113] P. Stein,et al. Porphyrin core expansion and doming in heme proteins. New evidence from resonance Raman spectra of six-coordinate high-spin iron(III) hemes , 1979 .
[114] Y. Kyōgoku,et al. Resonance Raman spectra of octaethylporphyrinato‐Ni(II) and meso‐deuterated and 15N substituted derivatives. II. A normal coordinate analysis , 1978 .
[115] Stephen P. Cramer,et al. Studies of the ferric forms of cytochrome P-450 and chloroperoxidase by extended x-ray absotption fine structure. Characterization of the iron-nitrogen and iron-sulfur distances , 1978 .
[116] Y. Hayashi,et al. Heme-linked ionization in compounds I and II of horseradish peroxidases A2 and C. , 1978, Archives of biochemistry and biophysics.
[117] T. Spiro,et al. Resonance Raman spectra and vibrational modes of iron(III) tetraphenylporphine .mu.-oxo dimer. Evidence for phenyl interaction and lack of dimer splitting , 1978 .
[118] S. Asher,et al. Resonance Raman spectra of methemoglobin derivatives. Selective enhancement of axial ligand vibrations and lack of an effect of inositol hexaphosphate. , 1977, Biochemistry.
[119] T. Spiro,et al. Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues. , 1976, Journal of the American Chemical Society.
[120] V. Gutmann. Empirical parameters for donor and acceptor properties of solvents , 1976 .
[121] Y. Kyōgoku,et al. Nature of the iron-ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering. , 1976, Journal of the American Chemical Society.
[122] V. Gutmann,et al. The acceptor number — A quantitative empirical parameter for the electrophilic properties of solvents , 1975 .
[123] H. Yamada,et al. Effects of 2,4-substituents of deuteropheme upon redox potentials of horseradish peroxidases. , 1975, Archives of biochemistry and biophysics.
[124] N. Yu,et al. Resonance Raman spectra of metallooctaethylporphyrins. Structural probe of metal displacement , 1975 .
[125] T. Spiro,et al. Resonance Raman spectra of heme proteins. Effects of oxidation and spin state. , 1974, Journal of the American Chemical Society.
[126] D. Dolphin,et al. THE CHEMISTRY OF PORPHYRIN π‐CATIONS * , 1973 .
[127] I. Salmeen,et al. The valence and spin state of iron in oxyhemoglobin as inferred from resonance Raman spectroscopy. , 1973, The Journal of biological chemistry.
[128] S. Klebanoff,et al. A PEROXIDASE-MEDIATED, STREPTOCOCCUS MITIS-DEPENDENT ANTIMICROBIAL SYSTEM IN SALIVA , 1973, The Journal of experimental medicine.
[129] D. Dolphin,et al. Compounds I of catalase and horse radish peroxidase: pi-cation radicals. , 1971, Proceedings of the National Academy of Sciences of the United States of America.
[130] D. Dolphin,et al. pi-Cation radicals and dications of metalloporphyrins. , 1970, Journal of the American Chemical Society.
[131] J. Pople,et al. Delocalization of Unpaired Electron Density of π Radicals into Substituent Phenyl Groups , 1968 .
[132] L. Alexander,et al. The molecular geometry of vanadyl deoxophylloerythroetioporphyrin. An analog of chlorophyll. , 1968, Journal of the American Chemical Society.
[133] Y. Chang,et al. The structure of the chromophore of sulphymyoglobin , 1967 .
[134] T. Yonetani,et al. Studies on cytochrome c peroxidase. VII. Electron paramagnetic resonance absorptions of the enzyme and complex ES in dissolved and crystalline forms. , 1966, The Journal of biological chemistry.
[135] D. Morris,et al. Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein. , 1966, The Journal of biological chemistry.
[136] L. Clarke,et al. THE HAEM PROSTHETIC GROUPS OF SOME ANIMAL PEROXIDASES. II. MYELOPEROXIDASE. , 1965, Biochimica et biophysica acta.
[137] J. Schultz,et al. MYELOPEROXIDASE OF THE LEUCOCYTE OF NORMAL HUMAN BLOOD. II. ISOLATION, SPECTROPHOTOMETRY, AND AMINO ACID ANALYSIS. , 1964, Biochemistry.
[138] H. A. Harbury. Oxidation-reduction potentials of horseradish peroxidase. , 1953, The Journal of biological chemistry.
[139] H. Theorell,et al. Magnetic properties of some peroxide compounds of myoglobin, peroxidase and catalase. , 1952, Archives of biochemistry and biophysics.
[140] D. Irvine,et al. The reaction between metmyoglobin and hydrogen peroxide. , 1952, The Biochemical journal.
[141] I. Morishima,et al. Preparation and Characterization of Oxoiron(IV) Chlorin Complexes as the First Models for a Reaction Intermediate in the Catalytic Cycle of Cytochrome d , 1994 .
[142] I. Morishima,et al. Preparation and characterization of an oxo–iron(V)–porphyrin complex , 1992 .
[143] Shen-ming Chen,et al. Electrochemical and spectral characterization of stable iron(IV) tetrakis-5,10,15,20-(N-methyl-4-pyridyl)porphyrin in aqueous solution at room temperature , 1990 .
[144] Xiaoyuan Li,et al. Consistent porphyrin force field. 1. Normal-mode analysis for nickel porphine and nickel tetraphenylporphine from resonance Raman and infrared spectra and isotope shifts , 1990 .
[145] T. J. Collins,et al. A water-stable manganese(V)-oxo complex: definitive assignment of a .nu.Mnv.tplbond.O infrared vibration , 1990 .
[146] M. Huber,et al. ENDOR studies of π-electron delocalization in covalently linked porphyrin dimers. Model systems for the primary donor in photosynthesis? , 1990 .
[147] John T. Groves,et al. Reactive iron porphyrin derivatives related to the catalytic cycles of cytochrome P-450 and peroxidase. Studies of the mechanism of oxygen activation , 1988 .
[148] J. Groves,et al. Oxomanganese(IV) porphyrins identified by resonance Raman and infrared spectroscopy. Weak bonds and the stability of the half-filled t2g subshell , 1988 .
[149] Y. Ozaki,et al. Infrared and Raman spectra of metalloporphyrins , 1987 .
[150] A. Salehi,et al. 鉄ポルフィリンπカチオンラジカル (OEP・+)FeIII(X)(X′)の溶液共鳴Ramanスペクトル , 1987 .
[151] R. Weiss,et al. Resonance Raman observation of the FeIVO stretching vibration in models for the active site of horse radish peroxidase compound II , 1986 .
[152] T. Spiro,et al. Resonance Raman spectroscopy as a probe of heme protein structure and dynamics. , 1985, Advances in protein chemistry.
[153] T. Kitagawa,et al. Resonance Raman Evidence for the Presence of the FeIV=O Bond in Horseradish Peroxidase Compound II , 1984 .
[154] F. Guengerich,et al. Chemical mechanisms of catalysis by cytochromes P-450: a unified view , 1984 .
[155] M. J. Coon,et al. Oxygen activation by cytochrome P-450. , 1980, Annual review of biochemistry.
[156] R. Bonnett,et al. Porphyrin N-oxides , 1978 .
[157] D. Dolphin,et al. Biochemical significance of porphyrin .pi. cation radicals , 1974 .