The oxygen-binding intermediates of human hemoglobin: evaluation of their contributions to cooperativity using zinc-containing hybrids.

PubWeight™: 0.83‹?›

🔗 View Article (PMC 1233676)

Published in Biophys J on October 01, 1996

Authors

Y Huang1, M L Doyle, G K Ackers

Author Affiliations

1: Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

Articles cited by this

Stereochemistry of cooperative effects in haemoglobin. Nature (1970) 13.71

Analytical gel chromatography of proteins. Adv Protein Chem (1970) 2.42

Molecular code for cooperativity in hemoglobin. Science (1992) 2.06

Coboglobins: oxygen-carrying cobalt-reconstituted hemoglobin and myoglobin. Proc Natl Acad Sci U S A (1970) 1.68

Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates. Biochemistry (1976) 1.62

Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves. Biochemistry (1976) 1.59

Reactions of haemoglobin dimers after ligand dissociation. Nature (1970) 1.59

Crystals of haemoglobin with the T quaternary structure bind oxygen noncooperatively with no Bohr effect. Nature (1991) 1.56

The linkage between oxygenation and subunit dissociation in human hemoglobin. Proc Natl Acad Sci U S A (1974) 1.51

Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins. J Biol Chem (1977) 1.47

Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin. Proc Natl Acad Sci U S A (1985) 1.34

A convenient chromatographic method for the preparation of human hemoglobin. Anal Biochem (1973) 1.29

Studies on cobalt myoglobins and hemoglobins. I. Preparation and optical properties of myoglobins and hemoglobins containing cobalt proto-, meso-, and deuteroporphyrins and thermodynamic characterization of their reversible oxygenation. J Biol Chem (1974) 1.28

Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin. Proc Natl Acad Sci U S A (1982) 1.28

Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect. J Biol Chem (1981) 1.27

Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers. Proteins (1992) 1.22

Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. Biochemistry (1985) 1.22

Measurement and analysis of ligand-linked subunit dissociation equilibria in human hemoglobins. Methods Enzymol (1981) 1.21

Oxygen binding by single crystals of hemoglobin. Biochemistry (1993) 1.16

Thermodynamic studies on the oxygenation and subunit association of human hemoglobin. Temperature dependence of the linkage between dimer-tetramer association and oxygenation state. J Biol Chem (1979) 0.94

Subunit hybridization studies of partially ligated cyanomethemoglobins using a cryogenic method. Evidence for three allosteric states. Biophys Chem (1990) 0.92

Oxygen binding by single crystals of hemoglobin: the problem of cooperativity and inequivalence of alpha and beta subunits. Proteins (1996) 0.90

Regulation of oxygen affinity by quaternary enhancement: does hemoglobin Ypsilanti represent an allosteric intermediate? Proteins (1992) 0.87

The energetics of ligand-linked subunit assembly in hemoglobin require a third allosteric structure. Biophys Chem (1990) 0.87

Single-site modifications of half-ligated hemoglobin reveal autonomous dimer cooperativity within a quaternary T tetramer. Proteins (1993) 0.87

Direct and indirect pathways of functional coupling in human hemoglobin are revealed by quantitative low-temperature isoelectric focusing of mutant hybrids. Biochemistry (1990) 0.86

Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin. Biochemistry (1992) 0.85

Three-state combinatorial switching in hemoglobin tetramers: comparison between functional energetics and molecular structures. Proc Natl Acad Sci U S A (1987) 0.85

Bohr effects of the partially-ligated (CN-met) intermediates of hemoglobin as probed by quaternary assembly. Biochemistry (1994) 0.84

Enthalpic and entropic components of cooperativity for the partially ligated intermediates of hemoglobin support a "symmetry rule" mechanism. Biochemistry (1995) 0.84

Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching. Proc Natl Acad Sci U S A (1991) 0.84

Oxygen equilibrium properties of nickel(II)-iron(II) hybrid hemoglobins cross-linked between 82 beta 1 and 82 beta 2 lysyl residues by bis(3,5-dibromosalicyl)fumarate: determination of the first two-step microscopic Adair constants for human hemoglobin. Biochemistry (1995) 0.84

Oxygen equilibrium properties of chromium (III)-iron (II) hybrid hemoglobins. J Biol Chem (1996) 0.83

Studies on cobalt myoglobins and hemoglobins X. Determination of microscopic oxygen-equilibrium constants of iron--cobalt hybrid hemoglobins and their parent hemoglobins. J Mol Biol (1980) 0.83

Transformation of cooperative free energies between ligation systems of hemoglobin: resolution of the carbon monoxide binding intermediates. Biochemistry (1996) 0.82

Metal-substituted hemoglobin and other hemoproteins. Methods Enzymol (1978) 0.82

Detection of hemoglobin hybrid formation at subzero temperature. Methods Enzymol (1981) 0.81

What the intermediate compounds in ligand binding to hemoglobin tell about the mechanism of cooperativity. Biophys Chem (1990) 0.81

Low-temperature electrophoresis methods. Methods Enzymol (1995) 0.80

Linkage between cooperative oxygenation and subunit assembly of cobaltous human hemoglobin. Biochemistry (1991) 0.80

Experimental resolution of cooperative free energies for the ten ligation species of cobalt(II)/iron(II)-CO hemoglobin. Biochemistry (1991) 0.79

Analysis of hemoglobin oxygenation from combined equilibrium and kinetic data. Is quaternary enhancement necessary? Biophys Chem (1990) 0.78

Heterometallic hybrids of homometallic human hemoglobins. Proc Natl Acad Sci U S A (1996) 0.78

Articles by these authors

The OR control system of bacteriophage lambda. A physical-chemical model for gene regulation. J Mol Biol (1985) 5.79

Quantitative model for gene regulation by lambda phage repressor. Proc Natl Acad Sci U S A (1982) 4.93

lambda Repressor and cro--components of an efficient molecular switch. Nature (1981) 4.52

Energetics of the HIV gp120-CD4 binding reaction. Proc Natl Acad Sci U S A (2000) 4.44

Quantitative DNase footprint titration: a method for studying protein-DNA interactions. Methods Enzymol (1986) 3.36

Analytical gel chromatography of proteins. Adv Protein Chem (1970) 2.42

"Footprint" titrations yield valid thermodynamic isotherms. Proc Natl Acad Sci U S A (1986) 2.35

Pyridinyl imidazole inhibitors of p38 mitogen-activated protein kinase bind in the ATP site. J Biol Chem (1997) 2.28

Identification and initial characterization of four novel members of the interleukin-1 family. J Biol Chem (2000) 2.24

Molecular code for cooperativity in hemoglobin. Science (1992) 2.06

Oxygenation-linked subunit interactions in human hemoglobin: analysis of linkage functions for constituent energy terms. Biochemistry (1976) 1.94

Energetics of cooperative protein-DNA interactions: comparison between quantitative deoxyribonuclease footprint titration and filter binding. Biochemistry (1986) 1.69

Temperature-sensitive differential affinity of TRAIL for its receptors. DR5 is the highest affinity receptor. J Biol Chem (2000) 1.68

Molecular sieve studies of interacting protein systems. I. Equations for transport of associating systems. J Biol Chem (1967) 1.62

Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates. Biochemistry (1976) 1.62

Hydrogen exchange measurement of the free energy of structural and allosteric change in hemoglobin. Science (1992) 1.60

Oxygenation-linked subunit interactions in human hemoglobin: experimental studies on the concentration dependence of oxygenation curves. Biochemistry (1976) 1.59

Free energy coupling within macromolecules. The chemical work of ligand binding at the individual sites in co-operative systems. J Mol Biol (1983) 1.55

Determination of the monomer-dimer equilibrium of interleukin-8 reveals it is a monomer at physiological concentrations. Biochemistry (1994) 1.53

New twists on an old story: hemoglobin. Trends Biochem Sci (1988) 1.52

The linkage between oxygenation and subunit dissociation in human hemoglobin. Proc Natl Acad Sci U S A (1974) 1.51

Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding II: cooperative interactions of cro dimers. J Mol Biol (2000) 1.47

Thermodynamic studies on subunit assembly in human hemoglobin. Temperature dependence of the dimer-tetramer association constants for oxygenated and unliganded hemoglobins. J Biol Chem (1977) 1.47

Self-assembly of bacteriophage lambda cI repressor: effects of single-site mutations on the monomer-dimer equilibrium. Biochemistry (1994) 1.43

Effects of site-specific amino acid modification on protein interactions and biological function. Annu Rev Biochem (1985) 1.42

Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry (1995) 1.41

Experimental resolution of cooperative free energies for the ten ligation states of human hemoglobin. Proc Natl Acad Sci U S A (1985) 1.34

Kinetic analysis of a protein antigen-antibody interaction limited by mass transport on an optical biosensor. Biophys Chem (1997) 1.32

Energetics of subunit dimerization in bacteriophage lambda cI repressor: linkage to protons, temperature, and KCl. Biochemistry (1991) 1.31

Dissection of the nucleotide and metal-phosphate binding sites in cAMP-dependent protein kinase. Biochemistry (1999) 1.29

The ABRF-MIRG'02 study: assembly state, thermodynamic, and kinetic analysis of an enzyme/inhibitor interaction. J Biomol Tech (2003) 1.29

Probing the energetics of proteins through structural perturbation: sites of regulatory energy in human hemoglobin. Proc Natl Acad Sci U S A (1982) 1.28

Thermodynamic studies on subunit assembly in human hemoglobin. Self-association of oxygenated chains (alphaSH and betaSH): determination of stoichiometries and equilibrium constants as a function of temperature. J Biol Chem (1977) 1.27

Mutual effects of protons, NaCl, and oxygen on the dimer-tetramer assembly of human hemoglobin. The dimer Bohr effect. J Biol Chem (1981) 1.27

Site-specific enthalpic regulation of DNA transcription at bacteriophage lambda OR. Biochemistry (1992) 1.27

The linkage between oxygenation and subunit dissociation in human hemoglobin. Consequences for the analysis of oxygenation curves. Biochemistry (1975) 1.25

A direct comparison of the activities of two humanized respiratory syncytial virus monoclonal antibodies: MEDI-493 and RSHZl9. J Infect Dis (1999) 1.24

Elimination of Fc receptor-dependent effector functions of a modified IgG4 monoclonal antibody to human CD4. J Immunol (2000) 1.23

Mutagenic dissection of hemoglobin cooperativity: effects of amino acid alteration on subunit assembly of oxy and deoxy tetramers. Proteins (1992) 1.22

Measurement and analysis of ligand-linked subunit dissociation equilibria in human hemoglobins. Methods Enzymol (1981) 1.21

Isolation of lambda repressor mutants with defects in cooperative operator binding. Biochemistry (1993) 1.17

Linked functions in allosteric proteins. Extension of the concerted (MWC) model for ligand-linked subunit assembly and its application to human hemoglobins. J Mol Biol (1981) 1.17

Coupled energetics of lambda cro repressor self-assembly and site-specific DNA operator binding I: analysis of cro dimerization from nanomolar to micromolar concentrations. Biochemistry (2000) 1.17

Alkaline Bohr effect of human hemoglobin Ao. J Mol Biol (1988) 1.16

Single-site mutations in the C-terminal domain of bacteriophage lambda cI repressor alter cooperative interactions between dimers adjacently bound to OR. Biochemistry (1994) 1.16

Determination of the equilibrium constants of associating protein systems. 3. Evaluation of the weight fraction of monomer from the weight-average partition coefficient (application to bovine liver glutamate dehydrogenase). Biochemistry (1969) 1.15

Calorimetric analysis of lambda cI repressor binding to DNA operator sites. Biochemistry (1995) 1.15

Oxygen binding constants for human hemoglobin tetramers. Biochemistry (1987) 1.09

Carbon monoxide binding to human hemoglobin A0. Biochemistry (1987) 1.09

Measurement of DNA-protein equilibria using gel chromatography: application to the HinfI restriction endonuclease. Biochemistry (1985) 1.07

Cooperativity mutants of bacteriophage lambda cI repressor: temperature dependence of self-assembly. Biochemistry (1996) 1.05

Thermodynamic analysis of human hemoglobins in terms of the Perutz mechanism: extensions of the Szabo--Karplus model to include subunit assembly. Biochemistry (1982) 1.03

Study of protein subunit association equilibria by elution gel chromatography. Methods Enzymol (1979) 1.03

Interpreting kinetic rate constants from optical biosensor data recorded on a decaying surface. Anal Biochem (1998) 1.00

Studies of protein ligand binding by gel permeation techniques. Methods Enzymol (1973) 1.00

Rational design of femtomolar inhibitors of isoleucyl tRNA synthetase from a binding model for pseudomonic acid-A. Biochemistry (2000) 1.00

Self-association of hemoglobin betaSH chains is linked to oxygenation. Proc Natl Acad Sci U S A (1978) 0.99

Energetics of subunit assembly and ligand binding in human hemoglobin. Biophys J (1980) 0.99

Steady-state kinetic characterization of substrates and metal-ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidases (type 2). Biochemistry (2001) 0.99

Quantitative study of protein association at picomolar concentrations: the lambda phage cl repressor. Anal Biochem (1991) 0.99

Hydropathic analysis of the non-covalent interactions between molecular subunits of structurally characterized hemoglobins. J Mol Biol (1997) 0.98

A quantitative model for the cooperative mechanism of human hemoglobin. Proc Natl Acad Sci U S A (1984) 0.97

The hemoglobin tetramer: a three-state molecular switch for control of ligand affinity. Annu Rev Biophys Biophys Chem (1987) 0.97

Calorimetric determination of the heat of oxygenation of human hemolgobin as a function of pH and the extent of reaction. Biochemistry (1974) 0.96

Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity. Biochemistry (1996) 0.96

Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid. J Biol Chem (2001) 0.95

Identification, substrate specificity, and inhibition of the Streptococcus pneumoniae beta-ketoacyl-acyl carrier protein synthase III (FabH). J Biol Chem (2001) 0.95

Modification of the Fc region of a primatized IgG antibody to human CD4 retains its ability to modulate CD4 receptors but does not deplete CD4(+) T cells in chimpanzees. Clin Immunol (2001) 0.94

Subunit association of enzyme I of the Salmonella typhimurium phosphoenolpyruvate: glycose phosphotransferase system. Temperature dependence and thermodynamic properties. J Biol Chem (1984) 0.94

Thermodynamic studies on the oxygenation and subunit association of human hemoglobin. Temperature dependence of the linkage between dimer-tetramer association and oxygenation state. J Biol Chem (1979) 0.94

Subunit hybridization studies of partially ligated cyanomethemoglobins using a cryogenic method. Evidence for three allosteric states. Biophys Chem (1990) 0.92

Energetics of oxygenation-linked subunit interactions in human hemoglobin. Biochem Biophys Res Commun (1976) 0.92

Carbon monoxide and oxygen binding to human hemoglobin F0. Biochemistry (1989) 0.92

Resolvability of Adair constants from oxygenation curves measured at low hemoglobin concentration. Biophys Chem (1977) 0.91

Quaternary enhancement in binding of oxygen by human hemoglobin. Proc Natl Acad Sci U S A (1979) 0.91

Proton-linked contributions to site-specific interactions of lambda cI repressor and OR. Biochemistry (1990) 0.90

Electrostatic contributions to the energetics of dimer-tetramer assembly in human hemoglobin: pH dependence and effect of specifically bound chloride ions. Biochemistry (1981) 0.90

Molecular sieve studies of interacting protein systems. V. Association of subunits of D-amino acid oxidase apoenzyme. Biochemistry (1969) 0.90

Expression, purification, and crystallization of the Escherichia coli selenomethionyl beta-ketoacyl-acyl carrier protein synthase III. Biochem Biophys Res Commun (2000) 0.90

Thermodynamic studies on ligand binding and subunit association of human hemoglobins. Enthalpies of binding O2 and CO to subunit chains of hemoglobin A. J Biol Chem (1979) 0.89

Oxygenation properties of the two co-occurring hemoglobins of the tube worm Riftia pachyptila. Respir Physiol (1990) 0.89

Functional properties of human hemoglobins synthesized from recombinant mutant beta-globins. Biochemistry (1992) 0.88

Thermodynamic studies on subunit assembly in human hemoglobin. Calorimetric measurements on the reconstitution of oxyhemoglobin from isolated chains. J Biol Chem (1977) 0.88

The pathway of allosteric control as revealed by hemoglobin intermediate states. FASEB J (1995) 0.88

Site-directed mutagenesis probing the catalytic role of arginines 165 and 166 of human cytomegalovirus protease. Biochemistry (1998) 0.87

Aspartokinase I-homoserine dehydrogenase I of Escherichia coli K12. Concentration-dependent dissociation to dimers in the presence of L-threonine. J Biol Chem (1978) 0.87

Regulation of oxygen affinity by quaternary enhancement: does hemoglobin Ypsilanti represent an allosteric intermediate? Proteins (1992) 0.87

Single-site modifications of half-ligated hemoglobin reveal autonomous dimer cooperativity within a quaternary T tetramer. Proteins (1993) 0.87

Molecular sieve studies of interacting protein systems. X. Behavior of small zone profiles for reversibly self-associating solutes. J Biol Chem (1971) 0.86

Molecular sieve studies of interacting protein systems. IV. Molecular size of the D-amino acid oxidase apoenzyme subunit. J Biol Chem (1969) 0.86

Direct and indirect pathways of functional coupling in human hemoglobin are revealed by quantitative low-temperature isoelectric focusing of mutant hybrids. Biochemistry (1990) 0.86

Effects of NaCl on the linkages between O2 binding and subunit assembly in human hemoglobin: titration of the quaternary enhancement effect. Biophys Chem (1997) 0.86

Cooperative non-specific DNA binding by octamerizing lambda cI repressors: a site-specific thermodynamic analysis. J Mol Biol (1998) 0.85

Equilibrium gel permeation: a single-photon counting spectrophotometer for studies of protein interaction. Biophys Chem (1976) 0.85

Molecular sieve studies of interacting protein systems. VI. Effects of axial dispersion on boundary profiles of associating macromolecules. J Biol Chem (1971) 0.85

Three-state combinatorial switching in hemoglobin tetramers: comparison between functional energetics and molecular structures. Proc Natl Acad Sci U S A (1987) 0.85

Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin. Biochemistry (1992) 0.85

Enthalpic and entropic components of cooperativity for the partially ligated intermediates of hemoglobin support a "symmetry rule" mechanism. Biochemistry (1995) 0.84

Identification of the intermediate allosteric species in human hemoglobin reveals a molecular code for cooperative switching. Proc Natl Acad Sci U S A (1991) 0.84