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In Memoriam
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Takashi Yonetani
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Department: Biochemistry and Biophysics
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Contact information
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206 Anatomy-Chemistry Building
Philadelphia, PA 19104-6059
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Philadelphia, PA 19104-6059
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Office: (215) 898-8787
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34 Fax: (215) 898-8559
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Email:
yonetant@mail.med.upenn.edu
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yonetant@mail.med.upenn.edu
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Publications
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Education:
21 9 B.S. 14 (Biology) c
31 Osaka University, Japan , 1953.
21 a Ph.D. 19 (Biochemistry) c
39 Osaka University, Japan with Professor Kazuo Okunuki 16 , 1960.
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Permanent link21 9 B.S. 14 (Biology) c
31 Osaka University, Japan , 1953.
21 a Ph.D. 19 (Biochemistry) c
39 Osaka University, Japan with Professor Kazuo Okunuki 16 , 1960.
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222 Dr. Yonetani investigates the structure-function correlations in hemoglobins, cytochromes, and peroxidases to elucidate the mechanism or action of these hemoglobins. Molecular structure, reactivity, and interactions of these hemoproteins with ligands, substrates, inhibitors, and allosteric effectors, are probed by chemical and genetical alterations of the molecular structure, EPR, NMR, FTIR, fluorescence, and resonance Raman examinations of the molecular structure as well as kinetic and thermodynamic measurements of their reactions.
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45 Dr. Yonetani's research interests are in the following areas:
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2d Ligand binding dynamics in myoglobin.
109 Chemical and genetical alterations of myoglobin, spectroscopic characterization of molecular structures, and kinetic and thermodynamic determination of ligand binding dynamics are used to elucidate the structural basis of the ligand reactivity in myoglobin.
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2b Allosteric mechanism in hemoglobin.
db Preparation of metal-substituted hybrid hemoglobins and chemically modified hemoglobins. Structure and function characterization of these modified hemoglobins to probe their allosteric and cooperative mechanism.
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3b The mechanism of action of cytochrome c peroxidase.
b6 The mode of interaction and the mechanism of electron transfer between cytochrome c peroxidase and cytochrome c are probed by transient kinetic and thermodynamic measurements.
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Description of Research Expertise
3a Description of Research Interests222 Dr. Yonetani investigates the structure-function correlations in hemoglobins, cytochromes, and peroxidases to elucidate the mechanism or action of these hemoglobins. Molecular structure, reactivity, and interactions of these hemoproteins with ligands, substrates, inhibitors, and allosteric effectors, are probed by chemical and genetical alterations of the molecular structure, EPR, NMR, FTIR, fluorescence, and resonance Raman examinations of the molecular structure as well as kinetic and thermodynamic measurements of their reactions.
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45 Dr. Yonetani's research interests are in the following areas:
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2d Ligand binding dynamics in myoglobin.
109 Chemical and genetical alterations of myoglobin, spectroscopic characterization of molecular structures, and kinetic and thermodynamic determination of ligand binding dynamics are used to elucidate the structural basis of the ligand reactivity in myoglobin.
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2b Allosteric mechanism in hemoglobin.
db Preparation of metal-substituted hybrid hemoglobins and chemically modified hemoglobins. Structure and function characterization of these modified hemoglobins to probe their allosteric and cooperative mechanism.
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3b The mechanism of action of cytochrome c peroxidase.
b6 The mode of interaction and the mechanism of electron transfer between cytochrome c peroxidase and cytochrome c are probed by transient kinetic and thermodynamic measurements.
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cf Yonetani, T., A. Tsuneshige and Y. Zhou : Interactions of nitric oxide (NO) with hemoproteins, particularly hemoglobion (Hb), as studied by EPR spectroscopy 35 MR Science 96: 63-67, 1999.
d6 Yonetani, T. : Structural and functional regulation of hemoglobin by nitric oxide as studied by EPR spectroscopy. Riken Rev. 24: 19-20, 1999.
13d Yonetani, T., A. Tsuneshige, Y.-X. Zhou and X.-S. Chen : Electron paramagnetic resonance and oxygen binding studies of a-nitrosyl hemoglobin: a novel oxygen carrier having NO-assisted allosteric functions. J. Biol. Chem. 273: 20323-20333, 1998.
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Selected Publications
154 Nagatomo, S., M. Nagai, A. Tsuneshige, T. Yonetani and T. Kitagawa: UV resonance Raman studies of a-nitrosyl hemoglobin derivatives: relation between the a1-b2 subunit interface interactions and the Fe-histidine bonding of the a heme. Biochemistry 38: 9659-66, 1999.cf Yonetani, T., A. Tsuneshige and Y. Zhou : Interactions of nitric oxide (NO) with hemoproteins, particularly hemoglobion (Hb), as studied by EPR spectroscopy 35 MR Science 96: 63-67, 1999.
d6 Yonetani, T. : Structural and functional regulation of hemoglobin by nitric oxide as studied by EPR spectroscopy. Riken Rev. 24: 19-20, 1999.
13d Yonetani, T., A. Tsuneshige, Y.-X. Zhou and X.-S. Chen : Electron paramagnetic resonance and oxygen binding studies of a-nitrosyl hemoglobin: a novel oxygen carrier having NO-assisted allosteric functions. J. Biol. Chem. 273: 20323-20333, 1998.
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