M. Tsubaki
Department of Life Science
Faculty of Science
Himeji Institute of Technology
Kamigoori-cho
Japan
Name/email consistency: high
- Diethyl pyrocarbonate modification abolishes fast electron accepting ability of cytochrome b561 from ascorbate but does not influence electron donation to monodehydroascorbate radical: identification of the modification sites by mass spectrometric analysis. Tsubaki, M., Kobayashi, K., Ichise, T., Takeuchi, F., Tagawa, S. Biochemistry (2000)
- Fourier-transform infrared studies on azide-binding to the binuclear center of the Escherichia coli bo-type ubiquinol oxidase. Tsubaki, M., Mogi, T., Hori, H. FEBS Lett. (1999)
- Fluoride-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption and EPR spectroscopies. Tsubaki, M., Mogi, T., Hori, H. J. Biochem. (1999)
- Azide- and cyanide-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption, EPR and FTIR spectroscopies. Tsubaki, M., Mogi, T., Hori, H. J. Biochem. (1999)
- 20beta-hydroxy-C21-steroid 20beta-oxidase activity of cytochrome P450c21 purified from bovine adrenocortical microsomes. Tsubaki, M., Matsumoto, N., Tomita, S., Ichikawa, Y., Hori, H. Biochim. Biophys. Acta (1998)
- Resonance Raman, infrared, and EPR investigation on the binuclear site structure of the heme-copper ubiquinol oxidases from Acetobacter aceti: effect of the heme peripheral formyl group substitution. Tsubaki, M., Matsushita, K., Adachi, O., Hirota, S., Kitagawa, T., Hori, H. Biochemistry (1997)
- Glutamate-286 mutants of cytochrome bo-type ubiquinol oxidase from Escherichia coli: influence of mutations on the binuclear center structure revealed by FT-IR and EPR spectroscopies. Tsubaki, M., Hori, H., Mogi, T. FEBS Lett. (1997)