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Papers by Jonathan Wittenberg

Research paper thumbnail of Hydrogen Sulfide Reduction of Symbiont Cytochrome c552 in Gills of Solemya reidi (Mollusca)

The Biological Bulletin, Jun 1, 1992

Abstract. The gill of the protobranch clam Solemya reidi houses a dense population of intracellul... more Abstract. The gill of the protobranch clam Solemya reidi houses a dense population of intracellular symbiotic che-moautotrophic sulfur-oxidizing bacteria that fix carbon dioxide into sugars and supply the carbon nutrition of the host. The gill is divided into a bacteriocyte (cells with ...

Research paper thumbnail of Studies on the equilibria and kinetics of the reactions of peroxidase with ligands. II. The reaction of ferroperoxidase with oxygen

Journal of Biological Chemistry, Feb 25, 1967

Research paper thumbnail of Studies on the Equilibria and Kinetics of the Reactions of Peroxidases with Ligands. III. The Dissociation of Carbon Monoxide from Carbon Monoxide Ferro-Horseradish Peroxidase

Biochemistry Usa, 1967

... JONATHAN B. WITTENBERG,~ ROBERT W. NOBLE,§ BEATRICE A. WITTENBERG, ERALDO ANTONINI, MAURIZIO ... more ... JONATHAN B. WITTENBERG,~ ROBERT W. NOBLE,§ BEATRICE A. WITTENBERG, ERALDO ANTONINI, MAURIZIO BRUNORI, AND JEFFRIES WYMAN From the ... which have been studied by, among others, Theorell, Keilin and Hartree, Keilin and Mann, Chance, and George. ...

Research paper thumbnail of Reaction of Μycobacterium tuberculosis truncated hemoglobin o with hydrogen peroxide : Εvidence for peroxidaticactivityand formation of protein-based radicals

The Journal of Biological Chemistry, 2007

Research paper thumbnail of The amino acid sequence of hemoglobin II from the symbiont-harboring clam Lucina pectinata

J Protein Chem, 1991

The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino ac... more The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino acid residues, has a calculated Mm of 17,476, including heme and an acetylated N-terminal residue. It retains the invariant residues Phe 44 at position CD1 and His 65 at the proximal position F8, as well as the highly conserved Trp 15 at position A12 and Pro 38 at position C2. The most likely candidate for the distal residue at position E7, based on the alignment with other globins, is Gln 65. However, optical and EPR spectroscopic studies of the ferri Hb II (Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J., J. Biol. Chem. 265, 16054-16059, 1990) have implicated a tyrosinate oxygen as the distal ligand. Modeling of the Lucina Hb II sequence, using the crystal structure of sperm whale aquometmyoglobin, showed that Tyr 30 substituting for the Leu located at position B10 can place its oxygen within 2.8 A of the water molecule occupying the distal ligand position. This structural alteration is facilitated by the coordinate mutation of the residue at position CD4, from Phe 46 in the sperm whale myoglobin sequence to Leu 47 in Lucina Hb II.

Research paper thumbnail of Crystallization and preliminary data for the ferric form of hemoglobin I

J Mol Biol, 1991

Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina... more Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina pectinata has been crystallized in a form suitable for atomic resolution X-ray structural investigations. The crystals have been grown at pH 4.8, in 0.05 M-acetate buffer, using 2.6 M-ammonium sulfate as precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit cell constants a = 50.0 A, b = 38.6 A, c = 42.1 A, beta = 107.1 degrees, and contain one molecule (14,000 Mr) in the asymmetric unit. By means of single crystal microspectrophotometry it has been shown that the crystals contain the ferric form of L. pectinata "sulfide reactive" hemoglobin I. On the other hand, by careful control of the buffering medium composition, it has been possible to obtain stable crystals of the deoxy, oxy and sulfide forms of the protein.

Research paper thumbnail of The Reaction of Ferrous Ascaris Perienteric Fluid Hemoglobin with Hydrogen Peroxide

Journal of Biological Chemistry, Jun 25, 1972

Research paper thumbnail of The amino acid sequence of hemoglobin III from the symbiont-harboring clam Lucina pectinata

Journal of protein chemistry, 1993

The cytoplasmic hemoglobin III from the gill of the symbiont-harboring clam Lucina pectinata cons... more The cytoplasmic hemoglobin III from the gill of the symbiont-harboring clam Lucina pectinata consists of 152 amino acid residues, has a calculated Mm of 18,068, including heme, and has N-acetyl-serine as the N-terminal residue. Based on the alignment of its sequence with other vertebrate and nonvertebrate globins, it retains the invariant residues Phe45 at position CD1 and His98 at the proximal position F8, as well as the highly conserved Trp16 and Pro39 at positions A12 and C2, respectively. The most likely candidate for the distal residue at position E7 is Gln66. Lucina hemoglobin III shares 95 identical residues with hemoglobin II (J. D. Hockenhull-Johnson et al., J. Prot. Chem. 10, 609-622, 1991), including Tyr at position B10, which has been shown to be capable of entering the distal heme cavity and placing its hydroxyl group within a 2.8 A of the water molecule occupying the distal ligand position, by modeling the hemoglobin II sequence using the crystal structure of sperm wha...

Research paper thumbnail of A novel reaction of hemoglobin in invertebrate nerves. I. Observations on annelid and molluscan nerves

Biochimica et biophysica acta, Jan 29, 1965

Research paper thumbnail of Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands

The Journal of biological chemistry, Jan 25, 1990

Three hemoglobins have been isolated from the symbiont-harboring gill of the bivalve mollusc Luci... more Three hemoglobins have been isolated from the symbiont-harboring gill of the bivalve mollusc Lucina pectinata. Oxyhemoglobin I (Hb I), which may be called sulfide-reactive hemoglobin, reacts with hydrogen sulfide to form ferric hemoglobin sulfide in a reaction that may proceed by nucleophilic displacement of bound superoxide anion by hydrosulfide anion. Hemoglobins II and II, called oxygen-reactive hemoglobins, remain oxygenated in the presence of hydrogen sulfide. Hemoglobin I is monomeric; Hb II and Hb III self-associate in a concentration-dependent manner and form a tetramer when mixed. Oxygen binding is not cooperative. Oxygen affinities are all nearly the same, P50 = 0.1 to 0.2 Torr, and are independent of pH. Combination of Hb I with oxygen is fast; k'on = (estimated) 100-200 x 10(6) M-1 s-1. Combination of Hb II and Hb III with oxygen is slow: k'on = 0.4 and 0.3 x 10(6) M-1 s-1, respectively. Dissociation of oxygen from Hb I is fast relative to myoglobin: koff = 61 s-...

Research paper thumbnail of Partial Amino Acid Sequence of Hemoglobin II from Lucina pectinata

Structure and Function of Invertebrate Oxygen Carriers, 1991

Research paper thumbnail of A novel reaction of hemoglobin in invertebrate tissues II. Observations on molluscan muscle

Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965

Research paper thumbnail of The amino acid sequence of hemoglobin II from the symbiont-harboring clamLucina pectinata

Journal of Protein Chemistry, 1991

The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino ac... more The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino acid residues, has a calculated Mm of 17,476, including heme and an acetylated N-terminal residue. It retains the invariant residues Phe 44 at position CD1 and His 65 at the proximal position F8, as well as the highly conserved Trp 15 at position A12 and Pro 38 at position C2. The most likely candidate for the distal residue at position E7, based on the alignment with other globins, is Gln 65. However, optical and EPR spectroscopic studies of the ferri Hb II (Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J., J. Biol. Chem. 265, 16054-16059, 1990) have implicated a tyrosinate oxygen as the distal ligand. Modeling of the Lucina Hb II sequence, using the crystal structure of sperm whale aquometmyoglobin, showed that Tyr 30 substituting for the Leu located at position B10 can place its oxygen within 2.8 A of the water molecule occupying the distal ligand position. This structural alteration is facilitated by the coordinate mutation of the residue at position CD4, from Phe 46 in the sperm whale myoglobin sequence to Leu 47 in Lucina Hb II.

Research paper thumbnail of Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide

Proceedings of the National Academy of Sciences, 2002

Research paper thumbnail of Ligand kinetics of hemoglobin S containing erythrocytes

Proceedings of the National Academy of Sciences, 1977

Research paper thumbnail of Crystallization of a complex of hemoglobin components II and III of the symbiont-harboring clam Lucina pectinata

Journal of Molecular Biology, 1991

Diffraction data to 3.1 A resolution were collected on crystals of a complex of components II and... more Diffraction data to 3.1 A resolution were collected on crystals of a complex of components II and III of the cytoplasmic hemoglobin of the symbiont-harboring clam Lucina pectinata. The crystal system is tetragonal, a = 76.3 A, c = 153.1 A and the space group is P42212. The asymmetric unit probably contains a dimer of the tetrameric complex.

Research paper thumbnail of Crystallization and preliminary data for the ferric form of Lucina pectinata hemoglobin I

Journal of Molecular Biology, 1991

Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina... more Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina pectinata has been crystallized in a form suitable for atomic resolution X-ray structural investigations. The crystals have been grown at pH 4.8, in 0.05 M-acetate buffer, using 2.6 M-ammonium sulfate as precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit cell constants a = 50.0 A, b = 38.6 A, c = 42.1 A, beta = 107.1 degrees, and contain one molecule (14,000 Mr) in the asymmetric unit. By means of single crystal microspectrophotometry it has been shown that the crystals contain the ferric form of L. pectinata "sulfide reactive" hemoglobin I. On the other hand, by careful control of the buffering medium composition, it has been possible to obtain stable crystals of the deoxy, oxy and sulfide forms of the protein.

Research paper thumbnail of Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins

Journal of Inorganic Biochemistry, 2005

Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed i... more Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed in eubacteria, cyanobacteria, unicellular eukaryotes, and in higher plants, constituting a distinct group within the hemoglobin (Hb) superfamily. TrHbs display amino acid sequences 20-40 residues shorter than classical (non)vertebrate Hbs and myoglobins, to which they are scarcely related by sequence similarity. The trHb tertiary structure is based on a 2-on-2 alpha-helical sandwich, which represents a striking editing of the highly conserved 3-on-3 alpha-helical globin fold, achieved through deletion/truncation of alpha-helices and specific residue substitutions. Despite their 'minimal' polypeptide chain span, trHbs display an inner tunnel/cavity system held to support ligand diffusion to/from the heme distal pocket, accumulation of heme ligands within the protein matrix, and/or multiligand reactions. Moreover, trHbs bind and effectively stabilize the heme and recognize diatomic ligands (i.e., O2, CO, NO, and cyanide), albeit with varying thermodynamic and kinetic parameters. Here, structural bases for heme binding and diatomic ligand recognition by trHbs are reviewed.

Research paper thumbnail of Viscosity-dependent Relaxation Significantly Modulates the Kinetics of CO Recombination in the Truncated Hemoglobin TrHbN from Mycobacterium tuberculosis

Journal of Biological Chemistry, 2004

Research paper thumbnail of A Cooperative Oxygen Binding Hemoglobin from Mycobacterium tuberculosis. STABILIZATION OF HEME LIGANDS BY A DISTAL TYROSINE RESIDUE

Journal of Biological Chemistry, 2000

Research paper thumbnail of Hydrogen Sulfide Reduction of Symbiont Cytochrome c552 in Gills of Solemya reidi (Mollusca)

The Biological Bulletin, Jun 1, 1992

Abstract. The gill of the protobranch clam Solemya reidi houses a dense population of intracellul... more Abstract. The gill of the protobranch clam Solemya reidi houses a dense population of intracellular symbiotic che-moautotrophic sulfur-oxidizing bacteria that fix carbon dioxide into sugars and supply the carbon nutrition of the host. The gill is divided into a bacteriocyte (cells with ...

Research paper thumbnail of Studies on the equilibria and kinetics of the reactions of peroxidase with ligands. II. The reaction of ferroperoxidase with oxygen

Journal of Biological Chemistry, Feb 25, 1967

Research paper thumbnail of Studies on the Equilibria and Kinetics of the Reactions of Peroxidases with Ligands. III. The Dissociation of Carbon Monoxide from Carbon Monoxide Ferro-Horseradish Peroxidase

Biochemistry Usa, 1967

... JONATHAN B. WITTENBERG,~ ROBERT W. NOBLE,§ BEATRICE A. WITTENBERG, ERALDO ANTONINI, MAURIZIO ... more ... JONATHAN B. WITTENBERG,~ ROBERT W. NOBLE,§ BEATRICE A. WITTENBERG, ERALDO ANTONINI, MAURIZIO BRUNORI, AND JEFFRIES WYMAN From the ... which have been studied by, among others, Theorell, Keilin and Hartree, Keilin and Mann, Chance, and George. ...

Research paper thumbnail of Reaction of Μycobacterium tuberculosis truncated hemoglobin o with hydrogen peroxide : Εvidence for peroxidaticactivityand formation of protein-based radicals

The Journal of Biological Chemistry, 2007

Research paper thumbnail of The amino acid sequence of hemoglobin II from the symbiont-harboring clam Lucina pectinata

J Protein Chem, 1991

The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino ac... more The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino acid residues, has a calculated Mm of 17,476, including heme and an acetylated N-terminal residue. It retains the invariant residues Phe 44 at position CD1 and His 65 at the proximal position F8, as well as the highly conserved Trp 15 at position A12 and Pro 38 at position C2. The most likely candidate for the distal residue at position E7, based on the alignment with other globins, is Gln 65. However, optical and EPR spectroscopic studies of the ferri Hb II (Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J., J. Biol. Chem. 265, 16054-16059, 1990) have implicated a tyrosinate oxygen as the distal ligand. Modeling of the Lucina Hb II sequence, using the crystal structure of sperm whale aquometmyoglobin, showed that Tyr 30 substituting for the Leu located at position B10 can place its oxygen within 2.8 A of the water molecule occupying the distal ligand position. This structural alteration is facilitated by the coordinate mutation of the residue at position CD4, from Phe 46 in the sperm whale myoglobin sequence to Leu 47 in Lucina Hb II.

Research paper thumbnail of Crystallization and preliminary data for the ferric form of hemoglobin I

J Mol Biol, 1991

Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina... more Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina pectinata has been crystallized in a form suitable for atomic resolution X-ray structural investigations. The crystals have been grown at pH 4.8, in 0.05 M-acetate buffer, using 2.6 M-ammonium sulfate as precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit cell constants a = 50.0 A, b = 38.6 A, c = 42.1 A, beta = 107.1 degrees, and contain one molecule (14,000 Mr) in the asymmetric unit. By means of single crystal microspectrophotometry it has been shown that the crystals contain the ferric form of L. pectinata "sulfide reactive" hemoglobin I. On the other hand, by careful control of the buffering medium composition, it has been possible to obtain stable crystals of the deoxy, oxy and sulfide forms of the protein.

Research paper thumbnail of The Reaction of Ferrous Ascaris Perienteric Fluid Hemoglobin with Hydrogen Peroxide

Journal of Biological Chemistry, Jun 25, 1972

Research paper thumbnail of The amino acid sequence of hemoglobin III from the symbiont-harboring clam Lucina pectinata

Journal of protein chemistry, 1993

The cytoplasmic hemoglobin III from the gill of the symbiont-harboring clam Lucina pectinata cons... more The cytoplasmic hemoglobin III from the gill of the symbiont-harboring clam Lucina pectinata consists of 152 amino acid residues, has a calculated Mm of 18,068, including heme, and has N-acetyl-serine as the N-terminal residue. Based on the alignment of its sequence with other vertebrate and nonvertebrate globins, it retains the invariant residues Phe45 at position CD1 and His98 at the proximal position F8, as well as the highly conserved Trp16 and Pro39 at positions A12 and C2, respectively. The most likely candidate for the distal residue at position E7 is Gln66. Lucina hemoglobin III shares 95 identical residues with hemoglobin II (J. D. Hockenhull-Johnson et al., J. Prot. Chem. 10, 609-622, 1991), including Tyr at position B10, which has been shown to be capable of entering the distal heme cavity and placing its hydroxyl group within a 2.8 A of the water molecule occupying the distal ligand position, by modeling the hemoglobin II sequence using the crystal structure of sperm wha...

Research paper thumbnail of A novel reaction of hemoglobin in invertebrate nerves. I. Observations on annelid and molluscan nerves

Biochimica et biophysica acta, Jan 29, 1965

Research paper thumbnail of Hemoglobins of the Lucina pectinata/bacteria symbiosis. I. Molecular properties, kinetics and equilibria of reactions with ligands

The Journal of biological chemistry, Jan 25, 1990

Three hemoglobins have been isolated from the symbiont-harboring gill of the bivalve mollusc Luci... more Three hemoglobins have been isolated from the symbiont-harboring gill of the bivalve mollusc Lucina pectinata. Oxyhemoglobin I (Hb I), which may be called sulfide-reactive hemoglobin, reacts with hydrogen sulfide to form ferric hemoglobin sulfide in a reaction that may proceed by nucleophilic displacement of bound superoxide anion by hydrosulfide anion. Hemoglobins II and II, called oxygen-reactive hemoglobins, remain oxygenated in the presence of hydrogen sulfide. Hemoglobin I is monomeric; Hb II and Hb III self-associate in a concentration-dependent manner and form a tetramer when mixed. Oxygen binding is not cooperative. Oxygen affinities are all nearly the same, P50 = 0.1 to 0.2 Torr, and are independent of pH. Combination of Hb I with oxygen is fast; k'on = (estimated) 100-200 x 10(6) M-1 s-1. Combination of Hb II and Hb III with oxygen is slow: k'on = 0.4 and 0.3 x 10(6) M-1 s-1, respectively. Dissociation of oxygen from Hb I is fast relative to myoglobin: koff = 61 s-...

Research paper thumbnail of Partial Amino Acid Sequence of Hemoglobin II from Lucina pectinata

Structure and Function of Invertebrate Oxygen Carriers, 1991

Research paper thumbnail of A novel reaction of hemoglobin in invertebrate tissues II. Observations on molluscan muscle

Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1965

Research paper thumbnail of The amino acid sequence of hemoglobin II from the symbiont-harboring clamLucina pectinata

Journal of Protein Chemistry, 1991

The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino ac... more The cytoplasmic hemoglobin II from the gill of the clam Lucina pectinata consists of 150 amino acid residues, has a calculated Mm of 17,476, including heme and an acetylated N-terminal residue. It retains the invariant residues Phe 44 at position CD1 and His 65 at the proximal position F8, as well as the highly conserved Trp 15 at position A12 and Pro 38 at position C2. The most likely candidate for the distal residue at position E7, based on the alignment with other globins, is Gln 65. However, optical and EPR spectroscopic studies of the ferri Hb II (Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J., J. Biol. Chem. 265, 16054-16059, 1990) have implicated a tyrosinate oxygen as the distal ligand. Modeling of the Lucina Hb II sequence, using the crystal structure of sperm whale aquometmyoglobin, showed that Tyr 30 substituting for the Leu located at position B10 can place its oxygen within 2.8 A of the water molecule occupying the distal ligand position. This structural alteration is facilitated by the coordinate mutation of the residue at position CD4, from Phe 46 in the sperm whale myoglobin sequence to Leu 47 in Lucina Hb II.

Research paper thumbnail of Truncated hemoglobin HbN protects Mycobacterium bovis from nitric oxide

Proceedings of the National Academy of Sciences, 2002

Research paper thumbnail of Ligand kinetics of hemoglobin S containing erythrocytes

Proceedings of the National Academy of Sciences, 1977

Research paper thumbnail of Crystallization of a complex of hemoglobin components II and III of the symbiont-harboring clam Lucina pectinata

Journal of Molecular Biology, 1991

Diffraction data to 3.1 A resolution were collected on crystals of a complex of components II and... more Diffraction data to 3.1 A resolution were collected on crystals of a complex of components II and III of the cytoplasmic hemoglobin of the symbiont-harboring clam Lucina pectinata. The crystal system is tetragonal, a = 76.3 A, c = 153.1 A and the space group is P42212. The asymmetric unit probably contains a dimer of the tetrameric complex.

Research paper thumbnail of Crystallization and preliminary data for the ferric form of Lucina pectinata hemoglobin I

Journal of Molecular Biology, 1991

Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina... more Cytoplasmic monomeric hemoglobin I from the bacteria-harboring gill of the bivalve mollusc Lucina pectinata has been crystallized in a form suitable for atomic resolution X-ray structural investigations. The crystals have been grown at pH 4.8, in 0.05 M-acetate buffer, using 2.6 M-ammonium sulfate as precipitating agent. The crystals belong to the monoclinic space group P2(1), with unit cell constants a = 50.0 A, b = 38.6 A, c = 42.1 A, beta = 107.1 degrees, and contain one molecule (14,000 Mr) in the asymmetric unit. By means of single crystal microspectrophotometry it has been shown that the crystals contain the ferric form of L. pectinata "sulfide reactive" hemoglobin I. On the other hand, by careful control of the buffering medium composition, it has been possible to obtain stable crystals of the deoxy, oxy and sulfide forms of the protein.

Research paper thumbnail of Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins

Journal of Inorganic Biochemistry, 2005

Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed i... more Truncated hemoglobins (trHbs) are low-molecular-weight oxygen-binding heme-proteins distributed in eubacteria, cyanobacteria, unicellular eukaryotes, and in higher plants, constituting a distinct group within the hemoglobin (Hb) superfamily. TrHbs display amino acid sequences 20-40 residues shorter than classical (non)vertebrate Hbs and myoglobins, to which they are scarcely related by sequence similarity. The trHb tertiary structure is based on a 2-on-2 alpha-helical sandwich, which represents a striking editing of the highly conserved 3-on-3 alpha-helical globin fold, achieved through deletion/truncation of alpha-helices and specific residue substitutions. Despite their 'minimal' polypeptide chain span, trHbs display an inner tunnel/cavity system held to support ligand diffusion to/from the heme distal pocket, accumulation of heme ligands within the protein matrix, and/or multiligand reactions. Moreover, trHbs bind and effectively stabilize the heme and recognize diatomic ligands (i.e., O2, CO, NO, and cyanide), albeit with varying thermodynamic and kinetic parameters. Here, structural bases for heme binding and diatomic ligand recognition by trHbs are reviewed.

Research paper thumbnail of Viscosity-dependent Relaxation Significantly Modulates the Kinetics of CO Recombination in the Truncated Hemoglobin TrHbN from Mycobacterium tuberculosis

Journal of Biological Chemistry, 2004

Research paper thumbnail of A Cooperative Oxygen Binding Hemoglobin from Mycobacterium tuberculosis. STABILIZATION OF HEME LIGANDS BY A DISTAL TYROSINE RESIDUE

Journal of Biological Chemistry, 2000