Published in J Biol Chem on April 25, 1972
Purification and characterization of a bacterial nitrophenol oxygenase which converts ortho-nitrophenol to catechol and nitrite. J Bacteriol (1988) 1.88
Degradation of 2-hydroxybiphenyl and 2,2'-dihydroxybiphenyl by Pseudomonas sp. strain HBP1. Appl Environ Microbiol (1988) 1.52
Naphthalene degradation via salicylate and gentisate by Rhodococcus sp. strain B4. Appl Environ Microbiol (1992) 1.44
Steady-state kinetic analysis of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath). Biochem J (1986) 1.24
NahW, a novel, inducible salicylate hydroxylase involved in mineralization of naphthalene by Pseudomonas stutzeri AN10. J Bacteriol (1999) 1.17
Microbial metabolism of the pyridine ring. The hydroxylation of 4-hydroxypyridine to pyridine-3,4-diol (3,4-dihydroxypyridine) by 4-hydroxypyridine-3-hydroxylase. Biochem J (1974) 0.89
Degradation of 2-bromobenzoic acid by a strain of Pseudomonas aeruginosa. Appl Environ Microbiol (1990) 0.76
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
Preparation and properties of alpha- and beta-chains from human hemoglobin. J Biol Chem (1969) 2.37
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
Studies of a flavoprotein, salicylate hydroxylase. I. Preparation, properties, and the uncoupling of oxygen reduction from hydroxylation. J Biol Chem (1972) 1.88
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups. J Biol Chem (1973) 1.82
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
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
Siroheme: a new prosthetic group participating in six-electron reduction reactions catalyzed by both sulfite and nitrite reductases. Proc Natl Acad Sci U S A (1974) 1.48
Cavities and packing defects in the structural dynamics of myoglobin. EMBO Rep (2001) 1.47
The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J Biol Chem (1971) 1.44
The purification and some properties of electron transfer flavoprotein and general fatty acyl coenzyme A dehydrogenase from pig liver mitochondria. J Biol Chem (1975) 1.43
Functional aspects of the subunit association-dissociation equilibria of hemoglobin. J Biol Chem (1970) 1.42
Structural and functional effects of apolar mutations of the distal valine in myoglobin. J Mol Biol (1995) 1.37
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow. J Biol Chem (1974) 1.36
Cytochrome oxidase from Pseudomonas aeruginosa. I. Reaction with copper protein. Biochim Biophys Acta (1973) 1.34
Cytochrome P-450scc-substrate interactions. Studies of binding and catalytic activity using hydroxycholesterols. J Biol Chem (1982) 1.33
Properties of the T state of human oxyhemoglobin studies by laser photolysis. J Biol Chem (1977) 1.32
The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins. J Biol Chem (1971) 1.30
The effect of inositol hexaphosphate on the kinetics of CO and O 2 binding by human hemoglobin. 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
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
Spinach nitrite reductase. Purification and properties of a siroheme-containing iron-sulfur enzyme. J Biol Chem (1977) 1.25
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
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
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
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
Steroidogenic electron transport in adrenal cortex mitochondria. Mol Cell Biochem (1982) 1.09
Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism. J Biol Chem (1979) 1.08
Rates of reaction of Ascaris haemoglobins with ligands. Proc R Soc Lond B Biol Sci (1965) 1.06
Reaction of oxygen with cytochrome c oxidase from Paracoccus denitrificans. J Biol Chem (1981) 1.05
An iron tetrahydroporphyrin prosthetic group common to both assimilatory and dissimilatory sulfite reductases. Biochem Biophys Res Commun (1973) 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
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
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
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
Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef hart mitochondria. Arch Biochem Biophys (1976) 0.97
Studies on ligand binding to hemoglobins from teleosts and elasmobranchs. J Biol Chem (1973) 0.96
The role of diffusion in limiting the rate of ligand binding to hemoglobin. J Biol Chem (1980) 0.96
Kinetics of the incorporation of adrenal cytochrome P-450scc into phosphatidylcholine vesicles. J Biol Chem (1982) 0.96
Testing the two-state model: anomalous effector binding to human hemoglobin. Biochemistry (1986) 0.96
Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin. Proteins (1995) 0.96
The relation of pH and oxidation-reduction potential to the association state of the ferredoxin . ferredoxin:NADP+ reductase complex. J Biol Chem (1981) 0.95
A practical automatic data acquisition system for stopped-flow spectrophotometry. Comput Biomed Res (1969) 0.94
Mutation of residue Phe97 to Leu disrupts the central allosteric pathway in Scapharca dimeric hemoglobin. J Biol Chem (1997) 0.94
Mechanism of ligand binding to Ni(II)-Fe(II) hybrid hemoglobins. Biochemistry (1995) 0.94
The reaction of liver alcohol dehydrogenase with reduced diphosphopyridine nucleotide. J Biol Chem (1967) 0.94
Kinetic evidence for a tetrameric functional unit in hemoglobin. J Biol Chem (1968) 0.93
Kinetics of O2 and CO Binding to adrenal cytochrome P-450scc. Effect of cholesterol, intermediates, and phosphatidylcholine vesicles. J Biol Chem (1983) 0.93
Electron transfer by ferredoxin:NADP+ reductase. Rapid-reaction evidence for participation of a ternary complex. J Biol Chem (1984) 0.92
Trematode hemoglobins show exceptionally high oxygen affinity. Biophys J (1998) 0.92
The kinetics of ligand binding to hemoglobin valency hybrids and the effect of anions. J Biol Chem (1972) 0.92
Microsomal TPNH-cytochrome c reductase. Fed Proc (1966) 0.92
Reverse temperature dependence of tuna hemoglobin oxygenation. Biochem Biophys Res Commun (1977) 0.92
Protoheme-carbon monoxide geminate kinetics. Biochemistry (1986) 0.92
A kinetic description of ligand binding to sperm whale myoglobin. J Biol Chem (1986) 0.91
Conditions restricting allosteric transitions in carp hemoglobin. J Biol Chem (1973) 0.91
The reaction of carbon monoxide with horse hemoglobin in solution, in erythrocytes, and in crystals. J Biol Chem (1967) 0.91
Adrenodoxin reductase and adrenodoxin. Mechanisms of reduction of ferricyanide and cytochrome c. J Biol Chem (1977) 0.91
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
Nitric oxide recombination to double mutants of myoglobin: role of ligand diffusion in a fluctuating heme pocket. Biochemistry (1994) 0.90
Uncoupling of oxygen activation from hydroxylation in a bacterial salicylate hydroxylase. Biochem Biophys Res Commun (1970) 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
Anomalous ligand binding by a class of high spin c-type cytochromes. J Biol Chem (1973) 0.90
Restricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity. Biochemistry (2001) 0.89
Manganese-substituted hemoglobin and myoglobin. Ann N Y Acad Sci (1975) 0.89
The effect of pH on carbon monoxide binding to Menhaden hemoglobin. Allosteric transitions in a root effect hemoglobin. J Biol Chem (1978) 0.89
The reaction of methemoglobin with some ligands. J Biol Chem (1969) 0.89
Studies on carbon monoxide binding by shark haemoglobin. Biochem J (1981) 0.89
Ionic effects on adrenal steroidogenic electron transport. The role of adrenodoxin as an electron shuttle. J Biol Chem (1979) 0.89