High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin.

The origin of co-operativity in haemoglobin (Hb) resides in the reduced affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol can be liganded without the molecule switching to the R high affinity state. X-ray analysis of T-state alpha-oxy Hb and T-state met Hb has identified the structural basis for reduced affinity. The nature of the chemical tension at the haem environment is different in the alpha and beta haems. There are small but definite structural changes associated with ligation in the T-state: these prove to be mostly in the same direction as the larger changes that occur in the T-->R transition.

[1]  T. A. Jones,et al.  A graphics model building and refinement system for macromolecules , 1978 .

[2]  Michael Levitt,et al.  Refinement of Large Structures by Simultaneous Minimization of Energy and R Factor , 1978 .

[3]  Wayne A. Hendrickson,et al.  A restrained-parameter thermal-factor refinement procedure , 1980 .

[4]  E. Henry,et al.  Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect , 1991, Nature.

[5]  C Chothia,et al.  Haemoglobin: the structural changes related to ligand binding and its allosteric mechanism. , 1979, Journal of molecular biology.

[6]  M. Vijayan,et al.  The determination and refinement of heavy‐atom parameters in protein heavy‐atom derivatives. Some model calculations using acentric reflexions , 1971 .

[7]  M. Perutz.  Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery , 1970, Nature.

[8]  G. Fermi,et al.  Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2-5 A resolution: refinement of the atomic model. , 1975, Journal of molecular biology.

[9]  N. W. Isaacs,et al.  A method for fitting satisfactory models to sets of atomic positions in protein structure refinements , 1976 .

[10]  K. B. Ward,et al.  Structure of deoxyhemoglobin A crystals grown from polyethylene glycol solutions. , 1975, Journal of molecular biology.

[11]  J L Hoard,et al.  Stereochemistry of hemes and other metalloporphyrins. , 1971, Science.

[12]  Ben F. Luisi,et al.  Stereochemistry of cooperative mechanisms in hemoglobin , 1987 .

[13]  Zygmunt Derewenda,et al.  Structure of the liganded T state of haemoglobin identifies the origin of cooperative oxygen binding , 1988, Nature.

[14]  B. Shaanan,et al.  Structure of human oxyhaemoglobin at 2.1 A resolution. , 1983, Journal of molecular biology.

[15]  S. Phillips,et al.  Structure and refinement of oxymyoglobin at 1.6 A resolution. , 1980, Journal of molecular biology.

[16]  K. Nagai,et al.  Distal residues in the oxygen binding site of haemoglobin studied by protein engineering , 1987, Nature.

[17]  R. Liddington,et al.  Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution. , 1990, Acta Crystallographica Section B Structural Science.

[18]  L Anderson,et al.  Intermediate structure of normal human haemoglobin: methaemoglobin in the deoxy quaternary conformation. , 1973, Journal of molecular biology.

[19]  R. C. Agarwal.  A new least‐squares refinement technique based on the fast Fourier transform algorithm: erratum , 1978 .

[20]  J. Changeux,et al.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. , 1965, Journal of molecular biology.

[21]  R. Liddington,et al.  Bonding of molecular oxygen to T state human haemoglobin , 1984, Nature.

[22]  B. Hoffman,et al.  X-ray diffraction studies of a partially liganded hemoglobin, [α(FeII-CO)β(MnII)]2 , 1986 .

[23]  B. Luisi,et al.  Structure of deoxy-quaternary haemoglobin with liganded beta subunits. , 1990, Journal of molecular biology.

[24]  M. Perutz,et al.  The crystal structure of human deoxyhaemoglobin at 1.74 A resolution. , 1984, Journal of molecular biology.

[25]  A. Brzozowski,et al.  Crystallization of human oxyhaemoglobin from poly(ethylene glycol) solutions. , 1978, The Biochemical journal.