Published in J Biol Chem on September 10, 1969
Lack of allosterically controlled intramolecular transfer of nitric oxide from the heme to cysteine in the beta subunit of hemoglobin. Blood (2005) 2.17
Reactions involving superoxide and normal and unstable haemoglobins. Biochem J (1976) 1.66
Picosecond photodissociation and subsequent recombination processes in carbon monoxide hemoglobin. Proc Natl Acad Sci U S A (1978) 1.58
Kinetics of the alkaline tetramer leads to dimer dissociation in liganded human hemoglobin: a laser light-scattering stopped-flow study. Proc Natl Acad Sci U S A (1977) 1.44
On the state of the iron and the nature of the ligand in oxyhemoglobin. Proc Natl Acad Sci U S A (1970) 1.24
Oxidation of human haemoglobin by copper. Mechanism and suggested role of the thiol group of residue beta-93. Biochem J (1977) 1.22
Low NO concentration dependence of reductive nitrosylation reaction of hemoglobin. J Biol Chem (2012) 1.20
Protein dynamics. Comparative investigation on heme-proteins with different physiological roles. Biophys J (1991) 1.13
Reconstitution of native human hemoglobin from separated globin chains and alloplex intermediates. Proc Natl Acad Sci U S A (1977) 1.11
The interaction of inositol hexaphosphate with methaemoglobin. Biochem J (1973) 1.06
Structurally inherent antigenic sites. Localization of the antigenic sites of the alpha-chain of human haemoglobin in three host species by a comprehensive synthetic approach. Biochem J (1982) 1.00
Haemoglobin binding with haptoglobin. Unequivocal demonstration that the beta-chains of human haemoglobin bind to haptoglobin. Biochem J (1980) 0.95
Spectral differences between the alpha and beta heme groups within human deoxyhemoglobin. Proc Natl Acad Sci U S A (1976) 0.95
Antigenic structure of human haemoglobin. Localization of the antigenic sites of the beta-chain in three host species by synthetic overlapping peptides representing the entire chain. Biochem J (1986) 0.93
A study of the reaction of protoporphyrin IX with human globin. Biochem J (1974) 0.92
The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly. Antioxid Redox Signal (2010) 0.92
Structural and functional studies on hemoglobin Bethesda (alpha2beta2 145His), a varient associated with compensatory erythrocytosis. J Clin Invest (1972) 0.91
Kinetics of α-globin binding to α-hemoglobin stabilizing protein (AHSP) indicate preferential stabilization of hemichrome folding intermediate. J Biol Chem (2012) 0.90
α-Hemoglobin stabilizing protein (AHSP) markedly decreases the redox potential and reactivity of α-subunits of human HbA with hydrogen peroxide. J Biol Chem (2012) 0.87
Aggregation of normal and sickle hemoglobin in high concentration phosphate buffer. Biophys J (2004) 0.87
Nanosecond optical rotatory dispersion spectroscopy: application to photolyzed hemoglobin-CO kinetics. Biophys J (1995) 0.87
The effect of water on the rate of conformational change in protein allostery. Biophys J (2001) 0.86
Haemichrome formation from haemoglobin subunits by hydrogen peroxide. Biochem J (1978) 0.85
Oxygen equilibrium and kinetics of isolated subunits from hemoglobin Kansas. Proc Natl Acad Sci U S A (1973) 0.83
Hemoglobin stability: observations on the denaturation of normal and abnormal hemoglobins by oxidant dyes, heat, and alkali. J Clin Invest (1970) 0.83
Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study. J Am Chem Soc (2014) 0.83
Hemoglobin brigham (alpha2Abeta2100 Pro--Leu). Hemoglobin variant associated with familial erythrocytosis. J Clin Invest (1973) 0.82
The potential of Angeli's salt to decrease nitric oxide scavenging by plasma hemoglobin. Free Radic Biol Med (2008) 0.82
Haem degradation in human haemoglobin in vitro. Separation of the contribution of the alpha- and beta-subunits. Biochem J (1984) 0.82
Alpha-hemoglobin stabilizing protein (AHSP), a kinetic scheme of the action of a human mutant, AHSPV56G. J Biol Chem (2010) 0.81
Linking conformation change to hemoglobin activation via chain-selective time-resolved resonance Raman spectroscopy of protoheme/mesoheme hybrids. J Biol Inorg Chem (2009) 0.81
T cells specific for alpha-beta interface regions of hemoglobin recognize the isolated subunit but not the tetramer and indicate presentation without processing. Proc Natl Acad Sci U S A (1989) 0.81
Photodissociation of CO and O2 from alpha and beta hemoglobin chains studied by using picosecond absorption spectroscopy. Biophys J (1987) 0.81
Photodissociation of a (mu-peroxo)(mu-hydroxo)bis[bis(bipyridyl)-cobalt(III)] complex: a tool to study fast biological reactions involving O2. Proc Natl Acad Sci U S A (1995) 0.80
Nitroxyl accelerates the oxidation of oxyhemoglobin by nitrite. Nitric Oxide (2013) 0.80
Nanosecond time-resolved absorption studies of human oxyhemoglobin photolysis intermediates. Biophys J (1996) 0.79
Pathway and mechanism of pH dependent human hemoglobin tetramer-dimer-monomer dissociations. PLoS One (2013) 0.79
Multiple geminate ligand recombinations in human hemoglobin. Biophys J (2000) 0.79
Methine-bridge specificity of the coupled oxidation of myoglobin and haemoglobin with ascorbate. Biochem J (1970) 0.78
Circe's haemoglobins, pig-human hybrids: functional characterization and structural considerations. Biochem J (1998) 0.78
EPR spectroscopy of nitrite complexes of methemoglobin. Inorg Chem (2010) 0.77
Sickle hemoglobin polymer melting in high concentration phosphate buffer. Biophys J (1999) 0.77
Apparatus for rapid and sensitive spectrophotometry. Biochem J (1964) 4.79
The reaction of reduced cytochrome C oxidase with oxygen. J Biol Chem (1967) 2.41
Mapping the pathways for O2 entry into and exit from myoglobin. J Biol Chem (2000) 2.31
Quaternary conformational changes in human hemoglobin studied by laser photolysis of carboxyhemoglobin. J Biol Chem (1976) 2.11
Ligand migration in sperm whale myoglobin. Biochemistry (1997) 1.74
Determination of the oxygen-combining power of blood with the Barcroft differential manometer. J Physiol (1943) 1.72
Kinetic studies by fluorescence resonance energy transfer employing a double-labeled oligonucleotide: hybridization to the oligonucleotide complement and to single-stranded DNA. Biochemistry (1995) 1.58
Cooperativity in the dissociation of nitric oxide from hemoglobin. J Biol Chem (1976) 1.55
Ordered water molecules as key allosteric mediators in a cooperative dimeric hemoglobin. Proc Natl Acad Sci U S A (1996) 1.51
Cavities and packing defects in the structural dynamics of myoglobin. EMBO Rep (2001) 1.47
Kinetics of the alkaline tetramer leads to dimer dissociation in liganded human hemoglobin: a laser light-scattering stopped-flow study. Proc Natl Acad Sci U S A (1977) 1.44
The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J Biol Chem (1971) 1.44
Functional aspects of the subunit association-dissociation equilibria of hemoglobin. J Biol Chem (1970) 1.42
Deoxycytidylate aminohydrolase. I. Preparation and properties of the homogeneous enzyme. Biochemistry (1967) 1.38
Structural and functional effects of apolar mutations of the distal valine in myoglobin. J Mol Biol (1995) 1.37
Cytochrome oxidase from Pseudomonas aeruginosa. I. Reaction with copper protein. Biochim Biophys Acta (1973) 1.34
Properties of the T state of human oxyhemoglobin studies by laser photolysis. J Biol Chem (1977) 1.32
The effect of inositol hexaphosphate on the kinetics of CO and O 2 binding by human hemoglobin. J Biol Chem (1971) 1.30
The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins. J Biol Chem (1971) 1.30
Structural dynamics of ligand diffusion in the protein matrix: A study on a new myoglobin mutant Y(B10) Q(E7) R(E10). Biophys J (1999) 1.29
Donor-acceptor distance distributions in a double-labeled fluorescent oligonucleotide both as a single strand and in duplexes. Biochemistry (1995) 1.29
The kinetics of ligand binding and of the association-dissociation reactions of human hemoglobin. Properties of deoxyhemoglobin dimers. J Biol Chem (1971) 1.27
The rates of polymerization and depolymerization of sickle cell hemoglobin. Biochem Biophys Res Commun (1974) 1.26
The reaction of oxygen with hemoglobin and the kinetic basis of the effect of salt on binding of oxygen. J Biol Chem (1970) 1.24
Simultaneous binding and bending of promoter DNA by the TATA binding protein: real time kinetic measurements. Biochemistry (1996) 1.23
DNA bends in TATA-binding protein-TATA complexes in solution are DNA sequence-dependent. J Biol Chem (2001) 1.20
On the photosensitivity of liganded hemoproteins and their metal-substituted analogues. Proc Natl Acad Sci U S A (1978) 1.19
Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques. J Biol Chem (1990) 1.19
Functional properties of hemoglobin Kempsey. J Biol Chem (1974) 1.18
Studies of a flavoprotein, salicylate hydroxylse. I. Enzyme mechanism. J Biol Chem (1972) 1.17
The reactions of antibodies with hemeprotein antgens. The measurement of reaction kinetics and stoichiometry by fluorescence quenching. J Biol Chem (1969) 1.16
The effect of pH on the reactions of oxygen and carbon monoxide with the hemoglobin of the carp, Cyprinus carpio. J Biol Chem (1970) 1.16
Deoxycytidylate aminohydrolase. II. Kinetic properties. The activatory effect of deoxycytidine triphosphate and the inhibitory effect of deoxythymidine triphosphate. Biochemistry (1967) 1.16
Studies of the primary oxygen intermediate in the reaction of fully reduced cytochrome oxidase. J Biol Chem (1991) 1.15
Quaternary conformational changes in human oxyhemoglobin studied by laser photolysis. J Biol Chem (1977) 1.14
Distal cavity fluctuations in myoglobin: protein motion and ligand diffusion. Biochemistry (1996) 1.14
Kinetics of ligand binding and quaternary conformational change in the homodimeric hemoglobin from Scapharca inaequivalvis. J Biol Chem (1984) 1.11
Photodissociation of ligands from heme and heme proteins. Effect of temperature and organic phosphate. J Biol Chem (1977) 1.11
The reaction of n-butyl isocyanide with human hemoglobin. II. The ligand-binding properties of the and chains within deoxyhemoglobin. J Biol Chem (1972) 1.10
Observations on rapidly reacting hemoglobin. J Biol Chem (1967) 1.10
The association of NADPH with the guanine nucleotide exchange factor from rabbit reticulocytes: a role of pyridine dinucleotides in eukaryotic polypeptide chain initiation. Proc Natl Acad Sci U S A (1986) 1.08
Intermediate species possessing bent DNA are present along the pathway to formation of a final TBP-TATA complex. J Mol Biol (1999) 1.07
Rates of reaction of Ascaris haemoglobins with ligands. Proc R Soc Lond B Biol Sci (1965) 1.06
Studies on the role of eukaryotic nucleotide exchange factor in polypeptide chain initiation. J Biol Chem (1984) 1.05
The reaction of n-butyl isocyanide with human hemoglobin. I. Determination of the kinetic parameters involved in the last step in ligand binding. J Biol Chem (1971) 1.05
Reaction of oxygen with cytochrome c oxidase from Paracoccus denitrificans. J Biol Chem (1981) 1.05
Relation between structure and function in Hemoglobin Chesapeake. Biochemistry (1967) 1.04
The contribution of the alpha and beta chains to the kinetics of oxygen binding to and dissociation from hemoglobin. Proc Natl Acad Sci U S A (1973) 1.04
Ligand binding and conformation change in the dimeric hemoglobin of the clam Scapharca inaequivalvis. J Biol Chem (1993) 1.04
A comparison of the geminate recombination kinetics of several monomeric heme proteins. J Biol Chem (1988) 1.03
A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties. Biochemistry (1999) 1.03
The mechanism of 1- and 2-electron transfers catalyzed by reduced triphosphopyridine nucleotide-cytochrome c reductase. J Biol Chem (1965) 1.02
The rates of combination of the isolated chains of human hemoglobin with oxygen. J Biol Chem (1969) 1.01
Marked stepwise differences within a common kinetic mechanism characterize TATA-binding protein interactions with two consensus promoters. J Biol Chem (2001) 1.01
Dependence of the quantum efficiency for photolysis of carboxyhemoglobin on the degree of ligation. J Biol Chem (1979) 1.01
Ligand binding and release of an analogue of 2,3-diphosphoglycerate from human hemoglobin. J Biol Chem (1972) 1.00
The reaction of ferrous horseradish peroxidase with hydrogen peroxide. J Biol Chem (1970) 1.00
Acute onset of esophageal duplication cyst in adult. Case report. G Chir (2009) 1.00
Kinetic and equilibrium properties of hemoglobin Kansas. J Biol Chem (1973) 0.99
Use of a fluorescent analogue of 2,3-diphosphoglycerate as a probe of human hemoglobin conformation during carbon monoxide binding. J Biol Chem (1971) 0.99
Distal pocket polarity in ligand binding to myoglobin: structural and functional characterization of a threonine68(E11) mutant. Biochemistry (1991) 0.98
The role of diffusion in limiting the rate of ligand binding to hemoglobin. J Biol Chem (1980) 0.96
Circular dichroism spectra of hemoglobins. Methods Enzymol (1981) 0.96
Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin. Proteins (1995) 0.96
Studies on ligand binding to hemoglobins from teleosts and elasmobranchs. J Biol Chem (1973) 0.96
Testing the two-state model: anomalous effector binding to human hemoglobin. Biochemistry (1986) 0.96
Neck node dissection in thyroid cancer. A review. G Chir (2010) 0.94
Mutation of residue Phe97 to Leu disrupts the central allosteric pathway in Scapharca dimeric hemoglobin. J Biol Chem (1997) 0.94
A practical automatic data acquisition system for stopped-flow spectrophotometry. Comput Biomed Res (1969) 0.94
The reaction of liver alcohol dehydrogenase with reduced diphosphopyridine nucleotide. J Biol Chem (1967) 0.94
Mechanism of ligand binding to Ni(II)-Fe(II) hybrid hemoglobins. Biochemistry (1995) 0.94
Kinetic evidence for a tetrameric functional unit in hemoglobin. J Biol Chem (1968) 0.93
Microsomal TPNH-cytochrome c reductase. Fed Proc (1966) 0.92
Protoheme-carbon monoxide geminate kinetics. Biochemistry (1986) 0.92
Reverse temperature dependence of tuna hemoglobin oxygenation. Biochem Biophys Res Commun (1977) 0.92
The kinetics of ligand binding to hemoglobin valency hybrids and the effect of anions. J Biol Chem (1972) 0.92
Trematode hemoglobins show exceptionally high oxygen affinity. Biophys J (1998) 0.92
Kinetics of ribosome dissociation and subunit association studied in a light-scattering stopped-flow apparatus. Biochemistry (1976) 0.91
Kinetic studies on the interaction of chain initiation factor 3 with 70 S Escherichia coli ribosomes and subunits. J Biol Chem (1982) 0.91
The reaction of carbon monoxide with horse hemoglobin in solution, in erythrocytes, and in crystals. J Biol Chem (1967) 0.91
Conditions restricting allosteric transitions in carp hemoglobin. J Biol Chem (1973) 0.91
A kinetic description of ligand binding to sperm whale myoglobin. J Biol Chem (1986) 0.91
Ultra-rapid quantitative isolation of specific transfer ribonucleic acids. A solid-phase method. Biochem Biophys Res Commun (1974) 0.90
The oxidation of 1-deuterated glucose by glucose oxidase. J Biol Chem (1967) 0.90
The binding of carbon monoxide to and chains in tetrameric mammalian hemoglobin. J Biol Chem (1971) 0.90
Movement of Fe with respect to the heme plane in the R-T transition of carp hemoglobin. An extended x-ray absorption fine structure study. J Biol Chem (1986) 0.90
Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket. Biochemistry (1994) 0.90
Hemoglobin Kinetics of the Galapagos Rift Vent Tube Worm Riftia pachyptila Jones (Pogonophora; Vestimentifera). Science (1981) 0.90
Contributions of residue 45(CD3) and heme-6-propionate to the biomolecular and geminate recombination reactions of myoglobin. Biochemistry (1991) 0.90
Detection of point mutations in DNA by fluorescence energy transfer. J Biomed Opt (1996) 0.90
Anomalous ligand binding by a class of high spin c-type cytochromes. J Biol Chem (1973) 0.90
DNA sequence-dependent differences in TATA-binding protein-induced DNA bending in solution are highly sensitive to osmolytes. J Biol Chem (2001) 0.90
Rapid preparation of native alpha and beta chains of human hemoglobin. Int J Biochem (1992) 0.89
The reaction of methemoglobin with some ligands. J Biol Chem (1969) 0.89