Correspondence of the pK values of oxyHb-titration states detected by resonance Raman scattering to kinetic data of ligand dissociation and association.

No abstract is available for this paper.

• Publication year

  1986

• Venue

  Biophysical Journal

• Publication date

  1986-05-01

• Fields of study

  Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0006-3495(86)83736-5PMID 3708092PMCID PMC1329688
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The quantum theory of light

  2024cited by this paper
• On the Hill plot of NMR data for titration of protein residues

  2004cited by this paper
• Involvement of His HC3(146)@ in the Bohr Effect of Human Hemoglobin STUDIES OF NATIVE AND N-ETHYLMALEIMIDE-TREATED HEMOGLOBIN A AND HEMOGLOBIN

  2001cited by this paper
• pH-dependent absorption in the B and Q bands of oxyhemoglobin and chemically modified oxyhemoglobin (BME) at low Cl- concentrations.

  1986cited by this paper
• Heme-apoprotein interaction in the modified oxyhemoglobin-bis(N-maleimidomethyl)ether and in oxyhemoglobin at high Cl-concentration detected by resonance Raman scattering.

  1985cited by this paper
• Haem-apoprotein interactions detected by resonance Raman scattering in Mb- and Hb-derivates lacking the saltbridge His146 beta-Asp94 beta.

  1985cited by this paper
• The pKa values of two histidine residues in human haemoglobin, the Bohr effect, and the dipole moments of alpha-helices.

  1985cited by this paper
• Quantitative evaluation for the role of beta 146 His and beta 143 His residues in the Bohr effect of human hemoglobin in the presence of 0.1 M chloride ion.

  1984cited by this paper
• Involvement of His HC3 (146) beta in the Bohr effect of human hemoglobin. Studies of native and N-ethylmaleimide-treated hemoglobin A and hemoglobin Cowtown (beta 146 His replaced by Leu).

  1984cited by this paper
• Structure of deoxyhemoglobin Cowtown [His HC3(146) beta----Leu]: origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin.

  1984cited by this paper
• Calculation of Error in Depolarization Ratio Measurement Due to Finite Collection Angle in Laser Raman Spectroscopy

  1984cited by this paper
• Investigation of protein induced changes of the electronic structure of iron in heme proteins by 1H NMR spectroscopy

  1984cited by this paper
• Identification of an allosterically sensitive unfolding unit in hemoglobin.

  1983influential reference
• Investigation of pH-induced symmetry distortions of the prosthetic group in oxyhaemoglobin by resonance Raman scattering

  1983cited by this paper
• Structure of human oxyhaemoglobin at 2.1 A resolution.

  1983cited by this paper
• The Monod-Wyman-Changeux allosteric model describes haemoglobin oxygenation with only one adjustable parameter.

  1983cited by this paper
• Comparison of the applicability of several allosteric models to the pH and 2,3-bis(phospho)glycerate dependence of oxygen binding by human blood.

  1982cited by this paper
• Control and pH dependence of ligand binding to heme proteins.

  1982cited by this paper
• A proton nuclear magnetic resonance investigation of histidyl residues in human normal adult hemoglobin.

  1982cited by this paper
• Strain and Electrostatic Contributions to Cooperativity in Hemoglobin

  1982cited by this paper
• The contribution of histidine (HC3) (146 beta) to the R state Bohr effect of human hemoglobin.

  1982cited by this paper
• The Effect of the 146β Histidine on the pH Dependence of the R State of Human Hemoglobin

  1982cited by this paper
• Resonance Raman and absorption spectroscopic detection of distal histidine--fluoride interactions in human methemoglobin fluoride and sperm whale metmyoglobin fluoride: measurements of distal histidine ionization constants.

  1981cited by this paper
• Role of the beta 146 histidyl residue in the alkaline Bohr effect of hemoglobin.

  1980cited by this paper
• Role of C-terminal histidine in the alkaline Bohr effect of human hemoglobin.

  1980cited by this paper
• Identification of residues contributing to the Bohr effect of human haemoglobin.

  1980influential reference
• Near-heme histidine residues of deoxy- and oxymyoglobins.

  1979cited by this paper
• Electrostatic effects in hemoglobin: Bohr effect and ionic strength dependence of individual groups.

  1979cited by this paper
• Electrostatic effects in hemoglobin: hydrogen ion equilibria in human deoxy- and oxyhemoglobin A.

  1979cited by this paper
• Tertiary structure variability within the quaternary states of hemoglobin: a spin label study.

  1978cited by this paper
• Studies on cobalt myoglobins and hemoglobins. Preparation of isolated chains containing cobaltous protoporphyrin IX and characterization of their equilibrium and kinetic properties of oxygenation and EPR spectra.

  1977cited by this paper
• Kinetic studies on the binding affinity of human hemoglobin for the 4th carbon monoxide molecule, L4.

  1976cited by this paper
• The effect of potassium chloride on the Bohr effect of human hemoglobin.

  1975cited by this paper
• PH dependence of the Adair constants of human hemoglobin. Nonuniform contribution of successive oxygen bindings to the alkaline Bohr effect.

  1975cited by this paper
• Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin.

  1974cited by this paper
• Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin.

  1974cited by this paper
• A general approach to co-operativity and its application to the oxygen equilibrium of hemoglobin and its effectors.

  1974influential reference
• Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin.

  1973cited by this paper
• Direct measurement of the pK values of an alkaline Bohr group in human hemoglobin.

  1973cited by this paper
• The effect of pH on the rates of ligand replacement reactions of human adult and fetal hemoglobins and their subunits.

  1972cited by this paper
• Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties.

  1971cited by this paper
• The Bohr Effect and Combination with Organic Phosphates

  1970cited by this paper
• Stereochemistry of cooperative effects in haemoglobin.

  1970cited by this paper
• ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

  1965cited by this paper

• Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility

  2014cites this paper
• Hemoglobin-ligand binding: understanding Hb function and allostery on atomic level.

  2011cites this paper
• Structure of relaxed-state human hemoglobin: insight into ligand uptake, transport and release.

  2009influential citation
• pH-induced conformational changes of the Fe2+-N,(His F8) linkage in deoxyhemoglobin trout IV detected by the Raman active Fe2+-N (His F8) stretching mode

  2005cites this paper
• Ttransition in oxyhemoglobin trout IV by resonance Raman scattering

  2005cites this paper
• Direct oxidation of haemoglobin at bare boron-doped diamond electrodes.

  2004cites this paper
• Polarization-sensitive resonance CSRS of deoxy-and oxyhaemoglobin

  1995cites this paper
• Raman dispersion spectroscopy probes heme distortions in deoxyHb-trout IV involved in its T-state Bohr effect.

  1993cites this paper
• Investigation of haem—protein coupling and structural heterogenity in myoglobin and haemoglobin by resonance Raman spectroscopy

  1992cites this paper
• Investigation of heme distortions and heme-protein coupling in the isolated subunits of oxygenated human hemoglobin by resonance Raman dispersion spectroscopy.

  1992cites this paper
• pH-induced conformational changes of the Fe(2+)-N epsilon (His F8) linkage in deoxyhemoglobin trout IV detected by the Raman active Fe(2+)-N epsilon (His F8) stretching mode.

  1992cites this paper
• Multimode analysis of depolarization ratio dispersion and excitation profiles of seven Raman fundamentals from the haeme group in ferrocytochrome c

  1991cites this paper
• Allosteric linkage-induced distortions of the prosthetic group in haem proteins as derived by the theoretical interpretation of the depolarization ratio in resonance Raman scattering

  1989cites this paper
• Detection of the heme perturbations caused by the quaternary R----T transition in oxyhemoglobin trout IV by resonance Raman scattering.

  1989cites this paper
• Highly resolved depolarization dispersion and excitation profiles of Raman fundamentals of protoporphyrin IX in a cytochrome c matrix

  1989cites this paper
• The influence of structural variations in the F- and FG-helix of the β-subunit modified oxyHb-NES on the heme structure detected by resonance Raman spectroscopy

  1989cites this paper
• Oxygen-organophosphate linkage in hemoglobin A. The double hump effect.

  1987cites this paper
• pH-dependent absorption in the B and Q bands of oxyhemoglobin and chemically modified oxyhemoglobin (BME) at low Cl- concentrations.

  1986cites this paper