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biochemistry and biophysics


Professor of Biochemistry and Biophysics

220 Anatomy-Chemistry Building/6059
T: (215) 898-8787 (Office)
T: (215) 898-7064 (Lab)
F: (215) 898-8559

Ph.D. Osaka University (1960)



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.

Dr. Yonetani's research interests are in the following areas:

Ligand binding dynamics in myoglobin
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.

Allosteric mechanism in hemoglobin
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.

The mechanism of action of cytochrome c peroxidase
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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