Connection between the Taxonomic Substates and Protonation of Histidines 64 and 97 in Carbonmonoxy Myoglobin

Alben, 1968, An infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonyls, Biochemistry, 7, 175, 10.1021/bi00841a022 Ansari, 1987, Rebinding and relaxation in the myoglobin pocket, Biophys. Chem., 26, 337, 10.1016/0301-4622(87)80034-0 Bai, 1995, Protein folding intermediates: native-state hydrogen exchange, Science, 269, 192, 10.1126/science.7618079 Balasubramanian, 1993, Perturbations of the distal heme pocket in human myoglobin mutants probed by infrared spectroscopy of bound CO: correlation with ligand binding kinetics, Proc. Natl. Acad. Sci. USA, 90, 4718, 10.1073/pnas.90.10.4718 Berendzen, 1990, Temperature-derivative spectroscopy: a tool for protein dynamics, Proc. Natl. Acad. Sci. USA, 87, 1, 10.1073/pnas.87.1.1 Braunstein, 1993, Ligand binding to heme proteins. III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin, Biophys. J., 65, 2447, 10.1016/S0006-3495(93)81310-9 Cheng, 1991, Neutron diffraction study of carbonmonoxy myoglobin, J. Mol. Biol., 220, 381, 10.1016/0022-2836(91)90020-7 Doster, 1982, Control and pH dependence of ligand binding to heme proteins, Biochemistry, 21, 4831, 10.1021/bi00263a001 Douzou, 1977 Englander, 1992, Hydrogen exchange measurements of the free energy of structural and allosteric change in hemoglobin, Science, 256, 1684, 10.1126/science.256.5064.1684 Frauenfelder, 1990, Proteins and pressure, J. Phys. Chem., 94, 1024, 10.1021/j100366a002 Frauenfelder, 1991, The energy landscapes and motions of proteins, Science, 254, 1598, 10.1126/science.1749933 Fuchsman, 1979, CO and O2 complexes of soybean leghemoglobins: pH effects upon infrared and visible spectra. Comparisons with CO and O2 complexes of myoglobin and hemoglobin, Biochemistry, 18, 1309, 10.1021/bi00574a030 Golub, 1983 Han, 1990, Metastable intermediates in myoglobin at low pH, Proc. Natl. Acad. Sci. USA, 87, 205, 10.1073/pnas.87.1.205 Hendler, 1994, Deconvolution based on the singular value decomposition and the pseudoinverse: a guide for beginners, J. Biochem. Biophys. Meth., 28, 1, 10.1016/0165-022X(94)90061-2 Henry, 1992, Singular value decomposition: Application to analysis of experimental data, 210 Hong, 1990, Conformational substates and motions in myoglobin: external influences on structure and dynamics, Biophys. J., 58, 429, 10.1016/S0006-3495(90)82388-2 Iben, 1989, Glassy behavior of a protein, Phys. Rev. Lett., 62, 1916, 10.1103/PhysRevLett.62.1916 Ivanov, 1994, Determination of CO orientation in myoglobin by single-crystal infrared linear dichroism, J. Am. Chem. Soc., 116, 4139, 10.1021/ja00088a084 Johnson, 1996, Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin, Biophys. J., 71, 1563, 10.1016/S0006-3495(96)79359-1 Kuriyan, 1986, X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Angstrom resolution, J. Mol. Biol., 192, 133, 10.1016/0022-2836(86)90470-5 Kushkuley, 1996, Theoretical study of the distal-side steric and electrostatic effects on the vibrational characteristics of the FeCO unit of the carbonylheme proteins and their models, Biophys. J., 70, 1214, 10.1016/S0006-3495(96)79680-7 Kushkuley, 1997, Theoretical study of the electrostatic and steric effects on the spectroscopic characteristics of the metal-ligand unit of heme proteins. 2. CO vibrational frequencies, 17O isotropic chemical shifts, and nuclear quadrupole coupling constants, Biophys. J., 72, 899, 10.1016/S0006-3495(97)78724-1 Li, 1994, Structural determinants of the stretching frequency of CO bound to myoglobin, Biochemistry, 33, 1433, 10.1021/bi00172a021 Li, 1988, Is bound CO linear or bent in heme proteins? Evidence from resonance Raman and infrared spectroscopic data, J. Am. Chem. Soc., 110, 6024, 10.1021/ja00226a017 Makinen, 1979, Structure of carboxymyoglobin in crystals and in solution, Proc. Natl. Acad. Sci. USA, 76, 6042, 10.1073/pnas.76.12.6042 Maxwell, 1976, An infrared study of NO bonding to heme B and hemoglobin A. Evidence for inositol hexaphospate induced cleavage of proximal histidine to iron bonds, Biochemistry, 15, 388, 10.1021/bi00647a023 Morikis, 1989, Resonance Raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement, Biochemistry, 28, 4791, 10.1021/bi00437a041 Mourant, 1993, Ligand binding to heme proteins. II. Transitions in the heme pocket of myoglobin, Biophys. J., 65, 1496, 10.1016/S0006-3495(93)81218-9 Müller, 1997 Nakamura, 1996, Roles of electrostatic interaction in proteins, Quart. Rev. Biophys., 29, 1, 10.1017/S0033583500005746 Nienhaus, 1994, Ligand binding to heme proteins. The effect of light on ligand binding in myoglobin, Biochemistry, 33, 13413, 10.1021/bi00249a030 Nienhaus, 1996, Protein dynamics, 15, 163 Nienhaus, 1998, Structural heterogeneity and ligand binding in carbonmonoxy myoglobin crystals at cryogenic temperatures, Biochemistry, 37, 6819, 10.1021/bi972843h Oldfield, 1991, A molecular model for the major conformational substates in heme proteins, J. Am. Chem. Soc., 113, 7537, 10.1021/ja00020a014 Ösapay, 1994, Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints, J. Mol. Biol., 244, 183, 10.1006/jmbi.1994.1718 Park, 1991, Biochemistry, 30, 2333, 10.1021/bi00223a007 Phillips, 1990, Crystal structure of myoglobin from a synthetic gene, Proteins Struct. Funct. Genet., 7, 358, 10.1002/prot.340070407 Potter, 1990, Infrared spectra of carbonyl hemoglobins: characterization of dynamic heme pocket conformers, Biochemistry, 29, 6283, 10.1021/bi00478a025 Press, 1992 Quillin, 1993, High resolution crystal structures of distal histidine mutants of sperm whale myoglobin, J. Mol. Biol., 234, 140, 10.1006/jmbi.1993.1569 Ramsden, 1989, Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide to myoglobin, Biochemistry, 28, 3125, 10.1021/bi00434a001 Ray, 1994, How far can proteins bend the FeCO unit? Distal polar effects in heme proteins and models, J. Am. Chem. Soc., 116, 162, 10.1021/ja00080a019 Sage, 1991, Spectroscopic studies of myoglobin at low pH: heme structure and ligation, Biochemistry, 30, 1227, 10.1021/bi00219a010 Sambrook, 1989 Shimada, 1982, Dynamic protein structures, J. Biol. Chem., 257, 11893, 10.1016/S0021-9258(18)33650-0 Shrager, 1982, Titration of individual components in a mixture with resolution of difference spectra, pKs, and redox transitions, Anal. Chem., 54, 1147, 10.1021/ac00244a031 Shrager, 1986, Chemical transitions measured by spectra and resolved using singular value decomposition, Chemom. Intell. Lab. Syst., 1, 59, 10.1016/0169-7439(86)80026-0 Springer, 1987, High-level expression of sperm whale myoglobin in Escherichia coli, Proc. Natl. Acad. Sci. USA, 84, 8961, 10.1073/pnas.84.24.8961 Springer, 1989, Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin, J. Biol. Chem., 264, 3057, 10.1016/S0021-9258(18)94029-9 Springer, 1994, Mechanisms of ligand recognition in myoglobin, Chem. Rev., 94, 699, 10.1021/cr00027a007 Strang, 1980 Tian, 1993, Investigations of ligand association and dissociaton rates in the “open” and “closed” states of myoglobin, J. Mol. Biol., 233, 155, 10.1006/jmbi.1993.1491 Tian, 1996, Probing heme protein conformational equilibration rates with kinetic selection, Biochemistry, 35, 3487, 10.1021/bi952474u Trotter, 1984, Eigenvalue distributions of large Hermitian matrices; Wigner’s semi-circle law and a theorem of Kac, Murdock and Szegö, Adv. Math., 54, 67, 10.1016/0001-8708(84)90037-9 Wigner, 1967, Random matrices in physics, SIAM Rev., 9, 1, 10.1137/1009001 Yang, 1996, Crystal structures of CO-, deoxy- and met-myoglobins at various pH values, J. Mol. Biol., 256, 762, 10.1006/jmbi.1996.0123 Young, 1991, Time- and temperature dependence of large-scale conformational transitions in myoglobin, Chem. Phys., 158, 315, 10.1016/0301-0104(91)87075-7 Zhu, 1992, Conformational interconversion in protein crystals, J. Mol. Biol., 224, 207, 10.1016/0022-2836(92)90584-7