Crystal structures of myoglobin-ligand complexes at near-atomic resolution.
暂无分享,去创建一个
J Berendzen | R M Sweet | I. Schlichting | J. Berendzen | J. Vojtěchovský | R. Sweet | K. Chu | I Schlichting | K Chu | J Vojtechovský
[1] ' BarryA.Springer,et al. Mechanisms of Ligand Recognition in Myoglobin , 2001 .
[2] Martha,et al. Ligand Binding to Heme Proteins , 2001 .
[3] G. Kachalova,et al. A steric mechanism for inhibition of CO binding to heme proteins. , 1999, Science.
[4] G. Nienhaus,et al. Structural heterogeneity and ligand binding in carbonmonoxy myoglobin crystals at cryogenic temperatures. , 1998, Biochemistry.
[5] Michael T. McMahon,et al. An experimental and quantum chemical investigation of CO binding to heme proteins and model systems: A unified model based on 13C, 17O, and 57Fe nuclear magnetic resonance and57Fe mossbauer and infrared spectroscopies , 1998 .
[6] T. Spiro,et al. Discordant Results on FeCO Deformability in Heme Proteins Reconciled by Density Functional Theory , 1998 .
[7] J. Olson,et al. EVIDENCE FOR HYDROGEN BONDING EFFECTS IN THE IRON LIGAND VIBRATIONS OF CARBONMONOXY MYOGLOBIN , 1998 .
[8] J B Findlay,et al. Protein dynamics derived from clusters of crystal structures. , 1997, Biophysical journal.
[9] J. Sage,et al. Structural characterization of the myoglobin active site using infrared crystallography. , 1997, Journal of molecular biology.
[10] Michele Parrinello,et al. Equilibrium Geometries and Electronic Structure of Iron−Porphyrin Complexes: A Density Functional Study , 1997 .
[11] H Frauenfelder,et al. Variations on a theme by Debye and Waller: From simple crystals to proteins , 1997, Proteins.
[12] E. Chien,et al. Spectroscopic effects of polarity and hydration in the distal heme pocket of deoxymyoglobin. , 1997, Biochemistry.
[13] Myoglobin and CO: structure, energetics, and disorder , 1997, JBIC Journal of Biological Inorganic Chemistry.
[14] A. Schmidt,et al. Freeze-Trapping Isomorphous Xenon Derivatives of Protein Crystals , 1997 .
[15] J. Prestegard,et al. NMR evidence for slow collective motions in cyanometmyoglobin , 1997, Nature Structural Biology.
[16] R. Hester,et al. A chemometric analysis of the resonance Raman spectra of mutant carbonmonoxy-myoglobins reveals the effects of polarity. , 1997, Biochimica et biophysica acta.
[17] S. Stavrov,et al. Theoretical study of the electrostatic and steric effects on the spectroscopic characteristics of the metal-ligand unit of heme proteins. 2. C-O vibrational frequencies, 17O isotropic chemical shifts, and nuclear quadrupole coupling constants. , 1997, Biophysical journal.
[18] G. Sheldrick,et al. SHELXL: high-resolution refinement. , 1997, Methods in enzymology.
[19] Z. Otwinowski,et al. Processing of X-ray diffraction data collected in oscillation mode. , 1997, Methods in enzymology.
[20] E. Garman,et al. Macromolecular Cryocrystallography , 1997 .
[21] T C Terwilliger,et al. Bayesian difference refinement. , 1996, Acta crystallographica. Section D, Biological crystallography.
[22] J. Olson,et al. Perturbation of the Fe−O2 Bond by Nearby Residues in Heme Pocket: Observation of νFe-O2 Raman Bands for Oxymyoglobin Mutants , 1996 .
[23] J. Olson,et al. Kinetic Pathways and Barriers for Ligand Binding to Myoglobin* , 1996, The Journal of Biological Chemistry.
[24] T C Terwilliger,et al. Bayesian weighting for macromolecular crystallographic refinement. , 1996, Acta crystallographica. Section D, Biological crystallography.
[25] James A. Ibers,et al. Structural Characterization of OC3OPor Capped Porphyrins: H2(OC3OPor), Fe(OC3OPor)(Cl), Fe(OC3OPor)(CO)(1-MeIm), and Fe(OC3OPor)(CO)(1,2-Me2Im) , 1996 .
[26] Mehul P. Patel,et al. Identification of Conformational Substates in Oxymyoglobin through the pH-Dependence of the Low-Temperature Photoproduct Yield , 1996 .
[27] J. Fettinger,et al. STRUCTURAL CHARACTERIZATION OF FIVE STERICALLY PROTECTED PORPHYRINS , 1996 .
[28] F. Yang,et al. Crystal structures of CO-, deoxy- and met-myoglobins at various pH values. , 1996, Journal of molecular biology.
[29] Hiroshi Nakatsuji,et al. Ground and excited states of oxyheme: SAC/SAC-CI study , 1996 .
[30] K S Wilson,et al. Ab initio determination of the crystal structure of cytochrome c6 and comparison with plastocyanin. , 1995, Structure.
[31] M. Lim,et al. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O , 1995, Science.
[32] M. Chance,et al. Structural and electronic factors that influence oxygen affinities: a spectroscopic comparison of ferrous and cobaltous oxymyoglobin. , 1995, Biochemistry.
[33] Teizo Kitagawa,et al. The Proximal Residue Largely Determines the CO Distortion in Carbon Monoxy Globin Proteins. An ab Initio Study of a Heme Prosthetic Unit , 1995 .
[34] S. Boxer,et al. A test of the role of electrostatic interactions in determining the CO stretch frequency in carbonmonoxymyoglobin. , 1995, Biochemical and biophysical research communications.
[35] P. Jewsbury,et al. Distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of three distal mutants. , 1995, Biophysical journal.
[36] G. Phillips,et al. Structure and dynamics of the water around myoglobin , 1995, Protein science : a publication of the Protein Society.
[37] L. Proniewicz,et al. Low frequency vibrational modes of oxygenated myoglobin, hemoglobins, and modified derivatives. , 1994, The Journal of biological chemistry.
[38] J. Fischer,et al. Structure-Reactivity Relationship in Oxygen and Carbon Monoxide Binding with Some Heme Models , 1994 .
[39] P. Jewsbury,et al. The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers. , 1994, Biophysical journal.
[40] Teizo Kitagawa,et al. THE PROXIMAL RESIDUE LARGELY DETERMINES THE CO DISTORTION IN CARBONMONOXY GLOBIN PROTEINS. AN AB INITIO STUDY OF A HEME PROSTHETIC UNIT , 1994 .
[41] P E Wright,et al. Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints. , 1994, Journal of molecular biology.
[42] I. Schlichting,et al. Crystal structure of photolysed carbonmonoxy-myoglobin , 1994, Nature.
[43] M. Chance,et al. Probing conformational changes upon photolysis: FTIR studies of the low temperature liganded and photoproduct states of oxy- and carbonmonoxymyoglobin , 1994 .
[44] M. Keim,et al. Determination of CO orientation in myoglobin by single-crystal infrared linear dichroism , 1994 .
[45] Christopher A. Reed,et al. Synthetic Heme Dioxygen Complexes , 1994 .
[46] S. Boxer,et al. Discovery of new ligand binding pathways in myoglobin by random mutagenesis , 1994, Nature Structural Biology.
[47] Michael L. Quillin,et al. Structural determinants of the stretching frequency of CO bound to myoglobin. , 1994, Biochemistry.
[48] J. Sessler,et al. How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models , 1994 .
[49] Michael L. Quillin,et al. High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. , 1994, Journal of molecular biology.
[50] K. Chu,et al. Structural heterogeneity in proteins at cryogenic temperatures. Cooling rate dependence , 1993 .
[51] J. Mourant,et al. Ligand binding to heme proteins: II. Transitions in the heme pocket of myoglobin. , 1993, Biophysical journal.
[52] Michael L. Quillin,et al. A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate. , 1994, The Journal of biological chemistry.
[53] A. Brünger. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures , 1992, Nature.
[54] J. B. Johnson,et al. Time- and temperature dependence of large-scale conformational transitions in myoglobin , 1991 .
[55] P. Wolynes,et al. The energy landscapes and motions of proteins. , 1991, Science.
[56] E. Oldfield,et al. A Molecular Model for the Major Conformational Substates in Heme Proteins , 1991 .
[57] D. Rinaldi,et al. An indo study of environment effects on the dioxygen position of an oxymyoglobin model , 1991 .
[58] B. Schoenborn,et al. Neutron diffraction study of carbonmonoxymyoglobin. , 1991, Journal of molecular biology.
[59] J. Ibers,et al. Structure of a carbon monoxide adduct of a capped porphyrin : Fe(C2-Cap)(CO)(1-methylimidazole) , 1991 .
[60] R. Huber,et al. Accurate Bond and Angle Parameters for X-ray Protein Structure Refinement , 1991 .
[61] E. Oldfield,et al. Distal and proximal ligand interactions in heme proteins: correlations between C-O and Fe-C vibrational frequencies, oxygen-17 and carbon-13 nuclear magnetic resonance chemical shifts, and oxygen-17 nuclear quadrupole coupling constants in C17O- and 13CO-labeled species. , 1991, Biochemistry.
[62] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[63] S. Yedgar,et al. The effect of the solvent viscosity on the migration of small molecules through the structure of myoglobin. , 1991, Biorheology.
[64] A T Brünger,et al. Slow-cooling protocols for crystallographic refinement by simulated annealing. , 1990, Acta crystallographica. Section A, Foundations of crystallography.
[65] M R Chance,et al. O2 and CO reactions with heme proteins: quantum yields and geminate recombination on picosecond time scales. , 1990, Biochemistry.
[66] Pál Ormos,et al. Proteins and pressure , 1990 .
[67] H. Frauenfelder. The Debye-Waller factor: From villain to hero in protein crystallography† , 1989 .
[68] J. Fettinger,et al. Structural characterization of a sterically encumbered iron(II) porphyrin CO complex , 1989 .
[69] S. Lin,et al. Orientation of carbon monoxide and structure-function relationship in carbonmonoxymyoglobin. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[70] T. Spiro,et al. Is bound carbonyl linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data. , 1988, Journal of the American Chemical Society.
[71] R. Hochstrasser,et al. Iron-carbonyl bond geometries of carboxymyoglobin and carboxyhemoglobin in solution determined by picosecond time-resolved infrared spectroscopy. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[72] D. Braga,et al. A mean-square displacement amplitude analysis of terminally bound CO groups in transition-metal clusters , 1988 .
[73] Jack D. Dunitz,et al. Interpretation of atomic displacement parameters from diffraction studies of crystals , 1988 .
[74] W. Caughey,et al. Oxygen infrared spectra of oxyhemoglobins and oxymyoglobins. Evidence of two major liganded O2 structures. , 1987, Biochemistry.
[75] J. B. Johnson,et al. Rebinding and relaxation in the myoglobin pocket. , 1987, Biophysical chemistry.
[76] M. Karplus,et al. Crystallographic R Factor Refinement by Molecular Dynamics , 1987, Science.
[77] D. Braga,et al. Treatment of light atoms in X-ray structural studies on metal carbonyl clusters: a critical view , 1987 .
[78] M Karplus,et al. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution. , 1986, Journal of molecular biology.
[79] H. Frauenfelder,et al. Ligand binding to heme proteins: relevance of low-temperature data. , 1986, Biochemistry.
[80] A. Bianconi,et al. Increase of the Fe effective charge in hemoproteins during oxygenation process. , 1985, Biochemical and biophysical research communications.
[81] B. Chance,et al. CO bond angle changes in photolysis of carboxymyoglobin. , 1984, Biochemistry.
[82] I. Kuntz,et al. Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A. , 1984, Biochemistry.
[83] J. D. Mcdonald,et al. Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures. , 1982, Proceedings of the National Academy of Sciences of the United States of America.
[84] B. Schoenborn,et al. Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobin. , 1981, Journal of molecular biology.
[85] Benno P. Schoenborn,et al. Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin , 1981, Nature.
[86] C. Reed,et al. A (carbonmonoxy)heme complex with a weak proximal bond. Molecular stereochemistry of carbonyl(deuteroporphinato)(tetrahydrofuran)iron(II). , 1981, Biochemistry.
[87] N. Yu,et al. Resonance Raman investigation of dioxygen bonding in oxycobaltmyoglobin and oxycobalthemoglobin: structural implication of splittings of the bound O--O stretching vibration. , 1981, Proceedings of the National Academy of Sciences of the United States of America.
[88] S. Phillips,et al. Structure and refinement of oxymyoglobin at 1.6 A resolution. , 1980, Journal of molecular biology.
[89] W. Caughey,et al. Structure of carboxymyoglobin in crystals and in solution. , 1979, Proceedings of the National Academy of Sciences of the United States of America.
[90] C. Appleby,et al. CO and O2 complexes of soybean leghemoglobins: pH effects upon infrared and visible spectra. Comparisons with CO and O2 complexes of myoglobin and hemoglobin. , 1979, Biochemistry.
[91] G J Williams,et al. The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1978, Archives of biochemistry and biophysics.
[92] M. Karplus,et al. Nature of the iron-oxygen bond in oxyhemoglobin. , 1977, Journal of the American Chemical Society.
[93] A. Allerhand,et al. Titration behavior and tautomeric states of individual histidine residues of myoglobins. Application of natural abundance carbon 13 nuclear magnetic resonance spectroscopy. , 1977, The Journal of biological chemistry.
[94] T. Takano,et al. Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. , 1977, Journal of molecular biology.
[95] T. Takano. Structure of myoglobin refined at 2-0 A resolution. II. Structure of deoxymyoglobin from sperm whale. , 1976, Journal of molecular biology.
[96] J. Ibers,et al. Stereochemistry of carbonylmetalloporphyrins. The structure of (pyridine)(carbonyl)(5, 10, 15, 20-tetraphenylprophinato)iron(II). , 1976, Journal of the American Chemical Society.
[97] A. Allerhand,et al. Titration behavior of individual tyrosine residues of myoglobins from sperm whale, horse, and red kangaroo. , 1976, The Journal of biological chemistry.
[98] W. Caughey,et al. An infrared study of nitric oxide bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds , 1976 .
[99] W. Caughey,et al. An infrared study of NO bonding to heme B and hemoglobin A. Evidence for inositol hexaphosphate induced cleavage of proximal histidine to iron bonds. , 1976, Biochemistry.
[100] J. Hofrichter,et al. Linear dichroism of biological chromophores. , 1976, Annual review of biophysics and bioengineering.
[101] H Frauenfelder,et al. Dynamics of ligand binding to myoglobin. , 1975, Biochemistry.
[102] A. Gupta. [Hemoglobin]. , 2018, Nihon Ketsueki Gakkai zasshi : journal of Japan Haematological Society.
[103] W. Caughey,et al. Elucidation of the mode of binding of oxygen to iron in oxyhemoglobin by in frared spectroscopy. , 1973, Biochemical and biophysical research communications.
[104] M. Brunori,et al. Enzyme Proteins. (Book Reviews: Hemoglobin and Myoglobin in Their Reactions with Ligands) , 1971 .
[105] K. N. Trueblood,et al. On the rigid-body motion of molecules in crystals , 1968 .
[106] J. Maling,et al. Interpretation of quadrupole splittings and isomer shifts in hemoglobin. , 1967, The Journal of chemical physics.
[107] G. Lang,et al. Mössbauer effect in some haemoglobin compounds , 1966 .
[108] JOSEPH J. WEISS,et al. Nature of the Iron–Oxygen Bond in Oxyhæmoglobin , 1964, Nature.
[109] V. Luzzati,et al. Traitement statistique des erreurs dans la determination des structures cristallines , 1952 .
[110] H. A. Liebhafsky,et al. X-Ray Absorption , 1949 .
[111] C. D. Coryell,et al. The Magnetic Properties and Structure of Hemoglobin, Oxyhemoglobin and Carbonmonoxyhemoglobin , 1936, Proceedings of the National Academy of Sciences.
[112] D. Drabkin,et al. SPECTROPHOTOMETRIC STUDIES III. METHEMOGLOBIN , 1935 .