Crystal structures of myoglobin-ligand complexes at near-atomic resolution.

[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 .