Spin Unpairing in Oxyand Carbonmonoxy-Hemoglobins

[1]  S. Vitale,et al.  Variability of the magnetic moment of carbon monoxide hemoglobin from carp. , 1980, Proceedings of the National Academy of Sciences of the United States of America.

[2]  Z. Herman,et al.  A theoretical investigation of the magnetic and ground-state properties of model oxyhemoglobin complexes , 1980 .

[3]  A. Desbois,et al.  Low-frequency vibrations in resonance Raman spectra of horse heart myoglobin. Iron-ligand and iron-nitrogen vibrational modes. , 1979, Biochemistry.

[4]  S. Vitale,et al.  Room-temperature magnetic properties of oxy- and carbonmonoxyhemoglobin. , 1978, Proceedings of the National Academy of Sciences of the United States of America.

[5]  M. Perutz,et al.  Interactions between the quaternary structure of the globin and the spin state of the heme in ferric mixed spin derivatives of hemoglobin. , 1978, Biochemistry.

[6]  M. Perutz,et al.  Influence of quaternary structure of the globin on thermal spin equilibria in different methemoglobin derivatives. , 1978, Biochemistry.

[7]  F. Parak,et al.  Mössbauer Spectroscopy on Oxygenated Sperm Whale Myoglobin: Evidence for an Fe3+-O2- Coupling at the Active Center , 1978, Zeitschrift fur Naturforschung. Section C, Biosciences.

[8]  G. Romani,et al.  Magnetic properties of oxyhemoglobin. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[9]  M. Perutz.  Structure and mechanism of haemoglobin. , 1976, British medical bulletin.

[10]  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.

[11]  M. Perutz,et al.  Influence of globin structures on the state of the heme. Ferrous low spin derivatives. , 1976, Biochemistry.

[12]  Q. Gibson,et al.  The origin of the Adams-Schuster difference spectrum of oxyhemoglobin. , 1975, Biochemical and biophysical research communications.

[13]  M. Brunori,et al.  Spectral changes and allosteric transition in trout haemoglobin , 1975, Nature.

[14]  T. M. Schuster,et al.  Phosphate-dependent spectroscopic changes in liganded hemoglobin. , 1974, Biochemical and biophysical research communications.

[15]  G. Lang,et al.  Mössbauer effect in some haemoglobin compounds , 1966 .

[16]  L. Pauling,et al.  Nature of the Iron–Oxygen Bond in Oxyhæmoglobin , 1964, Nature.

[17]  JOSEPH J. WEISS,et al.  Nature of the Iron–Oxygen Bond in Oxyhæmoglobin , 1964, Nature.

[18]  M. Brunori,et al.  STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. I. HUMAN HEMOGLOBIN. , 1964, The Journal of biological chemistry.

[19]  S. Vitale,et al.  Low Lying Paramagnetic States in Oxy- and Carbonmonoxyhemoglobins , 1981 .

[20]  M. Perutz,et al.  Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron. , 1979, Annual review of biochemistry.

[21]  J. V. Bannister,et al.  Oxygen-transport proteins , 1979 .

[22]  M. Brunori,et al.  Enzyme Proteins. (Book Reviews: Hemoglobin and Myoglobin in Their Reactions with Ligands) , 1971 .

[23]  D. W. Smith,et al.  The spectra of ferric haems and haemoproteins , 1970 .