Reactivity of ferric Aplysia and sperm whale myoglobins towards imidazole. X-ray and binding study.

[1]  M. Brunori,et al.  Absence of water at the sixth co-ordination site in ferric Aplysia myoglobin. , 1981, Journal of molecular biology.

[2]  K. Moffat,et al.  Structure of imidazole methemoglobin. , 1981, Journal of Molecular Biology.

[3]  M. Bolognesi,et al.  The crystal and molecular structure of two models of catalytic flavo(co)enzyme intermediates , 1978 .

[4]  G J Williams,et al.  The Protein Data Bank: a computer-based archival file for macromolecular structures. , 1977, Journal of molecular biology.

[5]  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.

[6]  A. Mozzarelli,et al.  Catalytic and regulatory properties of D-glyceraldehyde-3-phosphate dehydrogenase in the crystal. Spectral properties and chemical reactivity of a chromophoric acyl-enzyme intermediate. , 1977, Journal of molecular biology.

[7]  M. Perutz,et al.  Structure of horse carbonmonoxyhaemoglobin. , 1976, Journal of molecular biology.

[8]  K. Moffat,et al.  Structure of cyanide methemoglobin. , 1976, Journal of molecular biology.

[9]  T. Blundell,et al.  Crystallization and preliminary x-ray diffraction studies on met-myoglobin from Aplysia limacina. , 1975, Journal of molecular biology.

[10]  J. Davies,et al.  The crystal and molecular structure of unsolvated μ-oxo-bis[N,N'-ethylenebis(salicylaldiminato)iron(III)] , 1973 .

[11]  B. Matthews,et al.  The structure of thermolysin: an electron density map at 2-3 A resolution. , 1972, Journal of molecular biology.

[12]  Thomas A. Steitz,et al.  Structure of crystalline α-chymotrypsin: III. Crystallographic studies of substrates and inhibitors bound to the active site of α-chymotrypsin , 1969 .

[13]  B P Schoenborn,et al.  Structure of alkaline metmyoglobin-xenon complex. , 1969, Journal of molecular biology.

[14]  P. Bretscher Models for Haem-Haem Interaction , 1968, Nature.

[15]  F. S. Mathews,et al.  A semi-empirical method of absorption correction , 1968 .

[16]  B. Matthews Solvent content of protein crystals. , 1968, Journal of molecular biology.

[17]  M. Brunori,et al.  The transition between 'acid' and 'alkaline' ferric heme proteins. , 1968, Biochimica et biophysica acta.

[18]  J. Kendrew,et al.  Structure of Deoxymyoglobin : A Crystallographic Study , 1966, Nature.

[19]  R. Alberty,et al.  Temperature jump studies of sperm whale metmyoglobin. 3. Effect of heme-linked groups on ligand binding. , 1965, The Journal of biological chemistry.

[20]  R. G. Hart,et al.  Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution , 1960, Nature.

[21]  J. Kendrew,et al.  Imidazole Complexes of Myoglobin and the Position of the Hæm Group , 1955, Nature.

[22]  D. Irvine,et al.  Reactivity differences between haemoglobins, Part XI. The reaction of human methaemoglobin A and pigeon methaemoglobin with imidazole , 1968 .

[23]  B. F. Cameron,et al.  Absorption spectra of sperm-whale ferrimyoglobin. , 1966, The Biochemical journal.

[24]  J. Kendrew,et al.  THE MODE OF ATTACHMENT OF THE AZIDE ION TO SPERM WHALE METMYOGLOBIN. , 1964, Journal of molecular biology.

[25]  C. Tanford,et al.  The Consecutive Constants for the Association of Cadmium with Imidazole1, 2 , 1953 .