I. Original Papers

1. Assignment of the Fe-Ne(His F8) stretching band in the resonance Raman spectra of deoxymyoglobin, Kitagawa, T., K. Nagai, and M. Tsubaki, FEBS Lett., 104, 376-378, (1979).

2. Effect of removal of a salt-bridge on the oxygen binding properties and the electronic structure of heme in cobalt-iron hybrid hemoglobin, Tsubaki, M. and K. Nagai, J. Biochem., 86, 1029-1035, (1979).

3. Resonance Raman spectra of myoglobins reconstituted with spirographis and isospirographis hemes and iron 2,4-diformylprotoporphyrin IX. Effect of formyl substitution at the heme periphery, Tsubaki, M., K. Nagai, and T. Kitagawa, Biochemistry, 19, 379-385, (1980).

4. Resonance Raman spectra of manganese myoglobin and its azide complex. Assignment of a new charge-transfer band to azide(p) - porphyrin (p*) transition, Yu, N.-T. and M. Tsubaki, Biochemistry, 19, 4647-4653, (1980).

5. Temperature dependence of resonance Raman spectraof metmyoglobin and methemoglobin azide. Detection of resonance-enhancedbound azide vibrations and iron-azide stretch, Tsubaki, M., R. B. Srivastava, and N.-T. Yu. Biochemistry, 20, 946-952, (1981).

6. Resonance Raman investigation of dioxygen bondingin oxycobaltmyoglobin and oxycobalt-hemoglobin: Structural implication of splittings of the bound O-O stretching vibration, Tsubaki, M. and N.-T. Yu.. Proc. Natl. Acad. Sci. USA, 78, 3581-3585, (1981).

7. Resonance Raman investigation of carbon monoxide bonding in (carbonmonoxy) hemoglobin and -myoglobin: Detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change, Tsubaki,M., R. B. Srivastava, and N.-T. Yu, Biochemistry, 21, 1132-1140, (1982).

8. Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: Detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex, Tsubaki, M. and N.-T. Yu, Biochemistry, 21, 1140-1144, (1982).

9. Resonance Raman studies of Co-O2 and O-O stretching vibrations in oxy-cobalt hemes, Mackin,H. C., M. Tsubaki, and N.-T. Yu, Biophys.J., 41, 349-357, (1983).

10. Organ-specific properties of cytochromes P-450s21 (steroid 21-hydroxylases) of liver and adrenocortical microsomes, Ichikawa, Y., A. Hiwatashi, and M. Tsubaki, FEBS Lett., 167, 131-136,(1984).

11. Resonance Raman detection of a n(Fe-CO) stretching frequency in cytochrome P-450scc from bovine adrenocortical mitochondria, Tsubaki, M. and Y. Ichikawa, Biochim. Biophys. Acta, 827, 268-274, (1985).

12. Isolation and characterization of two constitutive forms of microsomal cytochrome P-450 from a single bovine liver, Tsubaki, M. and Y. Ichikawa, Biochim. Biophys. Acta, 830, 244-257,(1985).

13. Effects of cholesterol and adrenodoxin binding on the heme moiety of cytochrome P-450scc:A resonance Raman study, Tsubaki, M., A. Hiwatashi, and Y. Ichikawa, Biochemistry, 25, 3563-3569, (1986).

14. Characterization of two cysteine residues in cytochrome P-450scc: chemical identification of the heme-binding cysteine residue, Tsubaki, M., S. Tomita, Y. Tsuneoka, and Y. Ichikawa, Biochim. Biophys. Acta, 870, 564-574, (1986).

15. Effects of cholesterol analogues and inhibitors on the heme moiety of cytochrome P-450scc:A resonance Raman study, Tsubaki, M., A. Hiwatashi, and Y. Ichikawa, Biochemistry, 26, 4535-4540, (1987).

16. Electron paramagnetic resonance study of ferrouscytochrome P-450scc-nitric oxide complexes: Effects of cholesterol and itsanalogues, Tsubaki, M., A. Hiwatashi, Y. Ichikawa, and H. Hori, Biochemistry, 26, 4527-4534, (1987).

17. Influence of heme-surrounding amino acid residues on the manganese(V)-nitrido bond in manganese-substituted hemoproteins: Resonance Raman evidence for porphyrin core expansion and reduction of themanganese(V)-nitrido stretching force constant, Tsubaki, M., H. Hori, T. Hotta, A. Hiwatashi, Y. Ichikawa, and N.-T. Yu, Biochemistry, 26, 4980-4986, (1987).

18. Existence of multiple forms of cytochrome P-450scc purified from bovine adrenocortical mitochondria, Tsubaki, M., H. Ohkubo, Y. Tsuneoka, S. Tomita, A. Hiwatashi, and Y. Ichikawa, Biochim. Biophys. Acta, 914, 246-258, (1987).

19. Electron paramagnetic resonance study of ferrous cytochrome P-450scc-nitric oxide complexes: Effects of 20(R),22(R)-dihydroxycholesterol and reduced adrenodoxin, Tsubaki, M., A. Hiwatashi, Y. Fujimoto, N. Ikekawa, Y. Ichikawa, and H. Hori, Biochemistry, 27, 4856-4862, (1988) .

20. Crystallization of cytochrome P-450scc from bovine adrenocortical mitochondria, Iwamoto, Y., M. Tsubaki, A. Hiwatashi, and Y. Ichikawa, FEBS Lett., 233, 31-36,(1988).

21. Inhibition of electron transfer from adrenodoxinto cytochrome P-450scc by chemical modification with pyridoxal 5'-phosphate: Identification of adrenodoxin-binding site of cytochrome P-450scc, Tsubaki, M., Y. Iwamoto, A. Hiwatashi, and Y. Ichikawa, Biochemistry, 28, 6899-6907, (1989).

22. Conformational change of the heme moiety of ferrous cytochrome P-450scc-phenylisocyanide complex upon binding of reduced adrenodoxin, Tsubaki, M., A. Hiwatashi, and Y. Ichikawa, Biochemistry, 28, 9777-9784, (1989).

23. Studies of the immunohistochemical and biochemical localization of the cytochrome P-450scc-linked monooxygenase system inthe adult rat brain, Iwahashi, K., H. S. Ozaki, M. Tsubaki,J. Ohnishi, Y. Takeuchi, and Y. Ichikawa, Biochim. Biophys. Acta, 1035,182-189, (1990).

24. Active site of bovine adrenocortical cytochrome P-45011b studied by resonance Raman and electron paramagnetic resonance spectroscopies: Distinction from cytochrome P-450scc,Tsubaki, M., Y. Ichikawa, Y. Fujimoto, N.-T. Yu, and H. Hori, Biochemistry, 29, 8805-8812,(1990).

25. Purification and comparative characterization ofcytochrome P-450scc from porcine adrenocortical mitochondria, Iwahashi,K., M. Tsubaki, A. Miyatake, and Y. Ichikawa,Int. J. Biochem., 23, 901-909, (1991).

26. Light absorption, electron paramagnetic resonance and resonance Raman characteristics of nitridochromium(V) protoporphyrin-IX and its reconstitutedhemoproteins, Hori, H., M.Tsubaki,N.-T. Yu, and T. Yonetani, Biochim. Biophys. Acta, 1077, 392-399, (1991).

27. Cytochrome P-45011b in rat brain, Ozaki, H. S., K. Iwahashi, M. Tsubaki, Y. Fukui, Y. Ichikawa, and Y. Takeuchi, J. Neuroscience Res., 28, 518-524, (1991).

28. Catalytic properties of cytochrome P-450scc frombovine and porcine adrenocortical mitochondria: Effect of Tween 20 concentration, Iwahashi, K., M. Tsubaki, A. Miyatake, S. Miura, K. Hosokawa, and Y. Ichikawa, J. Steroid Biochem. Mol. Biol., 38, 727-731, (1991).

29. Electronic and stereochemical characterization of intermediates in the photolysis of ferric cytochrome P450scc nitrosyl complexes. Effects of cholesterol and its analogues on ligand binding structures, Hori, H., F. Masuya, M. Tsubaki, S. Yoshikawa, and Y. Ichikawa, J. Biol. Chem., 267, 18377-18381, (1992).

30. Effects of cholesterol side-chain groups and adrenodoxin binding on the vibrational modes of carbon monoxide bound to cytochrome P-450scc: Implications of the productive and nonproductive substrate bindings, Tsubaki, M., S. Yoshikawa, Y. Ichikawa, and N.-T. Yu, Biochemistry, 31, 8991-8999, (1992).

31. Effects of crystallization on the heme-carbon monoxide moiety of bovine heart cytochrome c oxidase carbonyl, Tsubaki, M., K. Shinzawa, and S. Yoshikawa, Biophys. J., 63, 1564-1571,(1992).

32. Absorbance spectral change of the cytochrome P-450S21-phenylisocyanide complex upon binding of reduced NADPH-cytochrome P-450 reductase, Iwamoto, Y., M. Tsubaki, S. Miura, and Y. Ichikawa, Biochim. Biophys. Acta, 1159, 122-128, (1992).

33. Fourier-transform infrared study of cyanide binding to Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: Implication of the redox-linked conformational change at the binuclear site, Tsubaki, M, Biochemistry, 32, 164-173, (1993).

34. Fourier-transform infrared study of azide binding to Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: New evidence for the redox-linked conformational change at the binuclear site, Tsubaki, M., Biochemistry, 32, 174-182, (1993).

35. Structure of the heme-copper binuclear center ofthe cytochrome bo complex of Escherichia coli: EPR and Fourier-transform infrared spectroscopic studies, Tsubaki, M., T. Mogi, Y. Anraku, and H. Hori, Biochemistry, 32, 6065-6072, (1993).

36. Identification of the functional domains in hemeO synthase: Site-directed mutagenesis studies on the cyoE gene of the cytochrome bo operon in Escherichia coli, Saiki, K., T. Mogi, H. Hori, M. Tsubaki, and Y. Anraku, J. Biol. Chem., 268, 26927-26934, (1993).

37. Cytochrome d axial ligand of the bd-type terminal quinol oxidase from Escherichia col,Tsubaki, M., T. Uno, H. Hori, T. Mogi, Y. Nishimura, and Y. Anraku, FEBS Lett., 335, 13-17, (1993).

38. Resonance Raman and Fourier-transform infrared studies on the subunit I histidine mutants of the cytochrome bo complex in Escherichia coli: Molecular structure of redox metal centers, Uno, T., T. Mogi, M. Tsubaki, Y. Nishimura, and Y. Anraku, J. Biol. Chem., 269, 11912-11920, (1994).

39. Purification and comparative characterization ofcytochrome P-450scc (CYP XIA1) from sheep adrenocortical mitochondria, Miyatake, A., M. Tsubaki, H. Hori, and Y. Ichikawa, Biochim. Biophys. Acta,1215, 176-182, (1994).

40. EPR studies on the photoproducts of ferric cytochromeP450cam (CYP101) nitrosyl complexes: Effects of camphor and its analogues on ligand-bound structures, Masuya, F., M. Tsubaki, R. Makino, and H. Hori, J. Biochem., 116, 1146-1152, (1994).

41. Molecular structure of redox metal centers of the cytochrome bo complex from Escherichia coli: Spectroscopic characterization of the subunit I histidine mutant oxidases, Tsubaki, M.,T. Mogi, H. Hori, T. Ogura, S. Hirota, T. Kitagawa, and Y. Anraku. J. Biol. Chem. 269, 30861-30868, (1994).

42. Tryptophan 2,3-dioxygenase in Saccharomyces cerevisiae, Iwamoto, Y., I. S. Matsui-Lee, M. Tsubaki, and R. Kido, Can. J. Microbiol., 41, 19-26, (1995).

43. Electron paramagnetic resonance investigation ofcytochrome P450c21 from bovine adrenocortical microsomes: a new enzymatic activity, Tsubaki, M., K. Morimoto, S.Tomita, S. Miura, Y. Ichikawa, A. Miyatake, F. Masuya, and H. Hori, Biochim. Biophys. Acta, 1259, 89-98, (1995).

44. Cyanide-binding site of bd-type ubiquinoloxidase from Escherichia coli, Tsubaki, M., H. Hori, T. Mogi, and Y. Anraku, J. Biol. Chem., 270, 28565-28569, (1995).

45. Infrared and EPR studies on cyanide-binding to the heme-copper binuclear center of cytochrome bo-type ubiquinol oxidase from Escherichia coli. Release of a CuB1+-cyano complex in the partially reduced state, Tsubaki, M., T. Mogi, H. Hori, M. Sato-Watanabe, and Y. Anraku, J. Biol. Chem., 271, 4017-4022, (1996).

46. EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli: The proximal axial ligand of heme d is nitrogenous amino acid residue, Hori, H., M. Tsubaki, T. Mogi, and Y. Anraku, J. Biol. Chem. 271, 9254-9258, (1996).

47. A tryptophan pyrrole-ring cleavage enzyme in the most primitive eukaryote, Iwamoto, Y.,I. S. Lee, M. Tsubaki, and R. Kido, Adv. Exp. Med. Biol. 398, 441-447, (1996).

48. Exploring subunit-subunit interactions in the Escherichia coli bo-type ubiquinol oxidase by extragenic suppressor mutation analysis, Saiki, K.,T. Mogi, M. Tsubaki, H. Hori, and Y. Anraku, J. Biol. Chem. 272, 14721-14726, (1997).

49. A novel chloride-binding site modulates the heme-copper binuclear center in the Escherichia coli bo-type ubiquinoloxidase, Hirano, T., T. Mogi, M. Tsubaki, H. Hori, Y. Orii, and Y. Anraku, J. Biochem., 122, 430-437, (1997).

50. Existence of two heme B centers in cytochrome b561 from bovine adrenal chromaffin vesicles as revealed by a new purification procedure and EPR spectroscopy, Tsubaki, M., M. Nakayama, E. Okuyama, Y. Ichikawa, and H. Hori, J. Biol. Chem. 272, 23206-23210, (1997).

51. Resonance Raman, FT-IR and EPR investigation on the binuclear site structure of the heme-copper ubiquinol oxidase from Acetobactor aceti: Effect of the heme peripheral group substitution, Tsubaki, M., K. Matsushita, O. Adachi, S. Hirota, T. Kitagawa, and H. Hori, Biochemistry, 36, 13034-13042, (1997).

52. 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., H. Hori, and T. Mogi, FEBS Lett., 416, 247-250, (1997).

53. 20b-Hydroxy-C21-steroid 20b-oxidase activities of cytochrome P450c21 purified from bovine adrenocortical microsomes, Tsubaki, M., N. Matsumoto, S. Tomita, Y. Ichikawa, and H. Hori, Biochim. Biophys. Acta, 1390, 197-206, (1997).

54. Substitutions of conserved aromatic amino acid residues in subunit I perturb the metal centers of the Escherichia coli bo-type ubiquinol oxidase, Mogi, T., J. Minagawa, T. Hirano, M. Sato-Watanabe, M. Tsubaki, T. Uno, H. Hori, H. Nakamura, Y. Nishimura, and Y. Anraku, Biochemistry, 37, 1632-1639, (1998).

55. Structural basis for the electron transfer across the chromaffin vesicle membranes catalyzed by cytochrome b561: Analyses of cDNA nucleotide sequences and visible absorption spectra, Okuyama, E., R. Yamamoto, Y.Ichikawa, and M. Tsubaki, Biochim. Biophys.Acta 1383, 269-278, (1998).

56. Distinct roles of two heme centers for transmembrane electron transfer in cytochrome b561 from bovine adrenal chromaffinvesicles as revealed by pulse radiolysis, Kobayashi, K., M.Tsubaki, and S. Tagawa, J. Biol. Chem. 273, 16038-16042, (1998).

57. Fourier-transform infrared studies on azide binding to the binuclear center of the Escherichia coli bo-type ubiquinol oxidase, Tsubaki, M., M. Mogi, and H. Hori, FEBS Lett., 449, 191-195, (1999).

58. Fluoride-binding to the Escherichia coli bd -type ubiquinol oxidase studied by visible absorption and EPR spectroscopies, Tsubaki, M., M. Mogi, and H. Hori, J. Biochem.,126, 98-103, (1999).

59. Azide- and cyanide-bindings to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption, EPR and FTIR spectroscopies, Tsubaki, M., M. Mogi, and H. Hori, J. Biochem.,126, 510-519, (1999).

60. Diethylpyrocarbonate-modification abolishes fast electron accepting ability of cytochrome b561 from ascorbate but does not influence on electron donation to monodehydroascorbate radical: Identification of the modification sites by mass spectrometric analyses, Tsubaki, M., K. Kobayashi, T. Ichise, F. Takeuchi, and S. Tagawa, Biochemistry, 39, 3276-3284, (2000).

61. Active site structure of SoxB-type cytochrome bo3 oxidase from thermophilic Bacillus, Uchida, T., M. Tsubaki, T. Kurokawa, H. Hori, J. Sakamoto, T. Kitagawa, N. Sone J. Inorg. Biochem. 82, 65-72, (2000).

62. Ascorbate inhibits the carbethoxylation of two histidyl and one tyrosyl residues indispensable for the transmembrane electron transfer reaction of cytochrome b561, Takeuchi, F., K. Kobayashi, S. Tagawa, and M. Tsubaki, Biochemistry, 40,4067-4076, (2001).

63. Unusual spin state equilibrium of azide metmyoglobin induced by core deformed heme, Neya, S.,Tsubaki, M., Hori, H., Yonetani, T., and Funasaki, N. Inorg. Chem., 40, 1220-1225, (2001).

64. Adrenodoxin-cytochrome P450scc interaction as revealed by EPR spectroscopy: Comparison with putidaredoxin-cytochrome P450cam system, Takeuchi, K., Tsubaki, M., Futagawa, J., Masuya, F. and Hori, H., J. Biochem. 130, 789-797 (2001).

65. Planarian cytochrome b561: Conservation of a six transmembrane structure and localization along the central and peripheral nervous system, Asada, A., Kusakawa, T., Orii, H., Agata, K., Watanabe, K., and Tsubaki, M., J. Biochem. 131, 175-182 (2002).

66. Cytochrome b561 is not fatty acylated but acetylated at the amino terminus in the chromaffin vesicle membranes: An approach for identification of the post-translational modification of membranous proteins, Nakamura M., Takeuchi F., and Tsubaki, M., Protoplasma 221, 41-46 (2003).

67. Stopped-flow analyses for the reaction of ascorbate with cytochrome b561 purified from bovine chromaffin vesicle membranes, Takigami, T., Takeuchi, F., Nakagawa, M., Hase, T., and Tsubaki, M., Biochemistry 42, 8110-8118 (2003).

68. Reversely-oriented cytochrome b561 in reconstituted vesicles catalyzes transmembrane electron transfer and supports extravesicular dopamine b-hydroxylase activity, Seike, Y., Takeuchi, F., and Tsubaki, M.,J. Biochem. 134,859-867 (2003).

69. Properties of two distinct heme centers of cytochrome b561 from bovine chromaffin vesicles studied by EPR, resonance Raman, and ascorbate reduction assay, Takeuchi, F., Hori, H., Obayashi, E., Shiro, Y., and Tsubaki, M., J. Biochem. 135,53-64 (2004).

70. Planarian peptidylglycine-hydroxylating monooxygenase, a neuropeptide processing enzyme,colocalizes with cytochrome b561 along the central nervous system. Asada, A., Orii, H., Watanabe, K., Tsubaki, M., FEBS Journal, 272, 942-955 (2005).

71. Cytochrome b561 Protein Family: Expanding Roles and Versatile Transmembrane Electron Transfer Abilities as Predicted by a New Classification System and Protein Sequence Motif Analyses, M. Tsubaki, F. Takeuchi, and N. Nakanishi, Biochim. Biophys. Acta, 1753, 174-190 (2005).

72. Selective perturbation of the intravesicular heme center of cytochrome b561 by cysteinyl modification with 4,4'-dithiodipyridine, F. Takeuchi, H. Hori, and M. Tsubaki, J. Biochem., 138, 751-762 (2005).

73. Protein-protein interaction of cytochrome b561 in chromaffin vesicle membranes studied by two-dimensional blue-native/sodium dodecyl sulfate gele electrophoresis and co-immunoprecipitation analysis, Takeuchi, F., Yamamoto, Y., Nishimura, Y., Park, S.-Y., and Tsubaki M., Acta Biologica Szegediensis, 50, 83-87 (2006).

74. Characterization of heme-coordinating histidyl residues of cytochrome b5 based on the reactivity with diethylpyrocarbonate: A mechanism for the opening of axial imidazole rings, Nobuyuki Nakanishi, Fusako Takeuchi, Hidetsugu Okamoto, Atsuo Tamura, Hiroshi Hori and Motonari Tsubaki, J. Biochem. 140, 561-571 (2006).

II. Reviews

1. Interactions between heme ligands and the protein moiety of heme-containing protein, H. Hori and M. Tsubaki, Seibutsubutsuri, 22, 151-159, (1982) (in Japanese).

2. Structural analysis of heme-copper terminal oxidases by infrared spectroscopy, M. Tsubaki, Seibutsubturi, 35, 107-112, (1995) (in Japanese).

3. Two terminal quinol oxidase families in Escherichia coli: Variations on molecular machinery for dioxygen reduction, Mogi, T., M. Tsubaki, H. Hori, H. Miyoshi, H. Nakamura, and Y. Anraku, J. Biochem. Mol. Biol. Bioiphys., 2, 79-110, (1998).

4. Probing molecular structure of dioxygen reduction site of bacterial quinol oxidases through ligand binding to the redox metal centers, Tsubaki, M., H. Hori, T. Mogi, J. Inorg. Biochem. 82, 19-25, (2000).

5. Transmembrane electron transfer catalyzed by cytochrome b561: Conserved properties and extending roles, Tsubaki, M. and F. Takeuchi, Rec. Res. Devel. Biochem., 4, 39-52, (2003).

6. Transmembrane electron transfer in the neuroendocrine vesicles: The ascorbate-cytochrome b561 system, Tsubaki, M., T. Takigami, Y. Seike and F. Takeuchi, Curr. Topics Biochem. Res., 5, 91-103,(2003).

III. Sections of Books

1. Multiple molecular forms and immunochemical properties of iron-sulfur proteins of mitochondria from bovine tissues, Ichikawa, Y., I. Hamamoto, N. Waki, K. Iwahashi, A. Hiwatashi, and M. Tsubaki, In "Iron-Sulfur Protein Research". H. Matsubara, editors, Japan Sci. Soc. Press, Tokyo, Springer-Verlag, Berlin, pp. 97-105, (1986).

2. Chemical modification of cytochrome P-450scc with pyridoxal 5'-phosphate: Inhibition of electron transfer from adrenodoxin, Tsubaki, M., K. Iwahashi, A. Hiwatashi, and Y. Ichikawa, In "Cytochrome P-450: Biochemistry and Biophysics". I. Schuster, editors. Taylor & Francis, London. pp. 387-390, (1989).

3. Effects of cholesterol side-chain groups and adrenodoxin-bindings on the vibrational modes of carbon monoxide bound to cytochrome P-450scc: Implications of the productive and nonproductive substrate bindings, Tsubaki, M., S. Yoshikawa, and N.-T. Yu, In "Cytochrome P-450: Biochemistry and Biophysics" A.I. Archakov and G.I. Bachmanova, editors. INCO-TNC Joint Stock Company, Moscow.pp. 177-179, (1991).

4. Fourier transform infrared study of cyanide binding to iron and copper sites of bovine heart cytochrome c oxidase, Tsubaki, M. and S. Yoshikawa.. In "Spectroscopy of Biological Molecules". R.E. Hester and R.B. Girling, editors. The Royal Society of Chemistry, Cambridge. pp. 269-270, (1991).

5. Heme-steroid interaction in cytochrome P450c21 studied by EPR and FTIR spectroscopies, Tsubaki, M., In "Molecular Steroidogenesis" M. Okamaoto, Y. Ishimura, H. Nawata, editors, Universal Academy Press, Inc., Tokyo, Japan, pp. 69-72, (2000).

6. Interaction of tail-anchored proteins with liposomes in different cholesterol content: Initial steps for the fabrication of artificial Neuroendocrine Vesicles, Jun Hamada, Nobuyuki Nakanishi, Fusako Takeuchi, Sam-Yong Park, and Motonari Tsubaki, 2006 International Symposium on Micro-NanoMechatronics and Human Science Symposium "Micro- and Nano-Mechatronics for Information-Based Society", The 21st Century COE Program, Nagoya University (M6048) (2006).

7. "Cytochrome b5", "cytochrome b561", "NADPH-ferrihemoprotein reductase", "cytochrome P-450", "cytochrome reductase", "microsomal electron transfer system", (in Japanese), Seikagakujiten, (4th edition), Tokyokagakudojin, (2007).

IV. Proceedings

1. Multichannel-detected resonance Raman spectra of manganese myoglobin and its azide complex, M. Tsubaki and N.-T. Yu, Proceedings VIIth international conference on Raman spectroscopy. (W.F. Murphy, editors) North-Holland, Amsterdam, New York, pp. 570-571,(1980).

2. Resonance Raman studies on heme-ligand bonding in hemoglobin and myoglobin: CO and CN bindings to heme iron, Motonari Tsubaki, Nai-Teng Yu, R. B. Srivastava, Proceedings of the 33th Symposium on Protein Structure(Osaka)(in Japanese), pp.41-44,(1982).

3. Resonance Raman spectra of cytochrome P-450scc from bovine adrenal cortex, M. Tsubaki, K. Matsusaka, and Y. Ichikawa, Proceedings of the IXth international conference on Raman spectroscopy, The Chemical Society of Japan,, Tokyo, pp. 752-753, (1984).

4. Resonance Raman detection of manganese-nitrogen triple bond. Formation of nitridomanganese(V) proto-porphyrin IX in manganese myoglobin, M. Tsubaki, H. Hori, T. Hotta, A. Hiwatashi, Y. Ichikawa, and N.-T. Yu, Proceedings of the Tenth International Conference on Raman Spectroscopy, University of Oregon, the University Printing Department, Eugene, Oregon, pp. 1-24 - 1-25, (1986)

5. Resonance Raman studies on structure and function of the reactive center of cytochrome P450scc, Motonari Tsubaki, Atsuo Hiwatashi, and Yoshiyuki Ichikawa, Proceedings of the 13th Symposium on Structure and Functions of Biological Molecules (Okazaki)(in Japanese), pp.45-46,(1986).

6. Physicochemical studies on the active site (heme) of cytochrome P-450 monooxygenase system, Motonari Tsubaki, The Naito Foundation Annual Reports 1986 (in Japanese), pp.90-91,(1986).

7. Interactions of cytochrome P-450scc(Fe2+-NO) complex with cholesterol and adrenodoxin: An EPR study, Motonari Tsubaki, Atsuo Hiwatashi, Yoshiyuki Ichikawa, and Hiroshi Hori, Proceedings of the 14th Symposium on Structure and Functions of Biological Molecules (Tokyo)(in Japanese), pp.57-58,(1987).

8. Molecular mechanism of the tromboxane A synthase inhibitors: Molecular properties as cytochrome P-450, Motonari Tsubaki, The Mochida Memorial Foundation Annual Research Reports (in Japanese), pp.153-157, (1988).

9. Similarities of the active site strucutures of E. coli cytochrome bo complex with mitochondrial cytochrome c oxidase: An infrared spectroscopic analysis, Motonari Tsubaki, Tatsushi Mogi, Shinya Yoshikawa, Yasuhiro Anraku, Proceedings of the 17th Annual Meeting of the Japanese Bioenergetics Group (Tokyo) (in Japanese), pp.32-33, (1991).

10. Structure of the binuclear metal center of the E. coli cytochrome bo complex: Analyses using EPR and infrared spectroscopies, Motonari Tsubaki, Shinya Yoshikawa, Hiroshi Hori, Tatsushi Mogi, and Yasuhiro Anraku, Proceedings of the 18th Annual Meeting of the Japanese Bioenergetics Group (Tokyo) (in Japanese), pp. 152-153, (1992).

11. Analysis of the proton pump mechanism of terminal oxidases using FT-IR and EPR spectroscopies, Motonari Tsubaki, Proceedings of the 19th Annual Meeting of the Japanese Bioenergetics Group (Toyonaka) (in Japanese), pp. 86-87, (1993).

12. A new steroid oxidase activity catalyszed by cytochrome P450c21 as revealed by EPR spectroscopic analysis, Motonari Tsubaki, Kohji Morimoto, Shuhei Tomita, Shigetoshi Miura, Yoshiyuki Ichikawa, Futoshi Masuya, and Hiroshi Hori, Proceedings of the 21th Symposium on Structure and Functions of Biological Molecules (Tokyo)(in Japanese), pp. 13-14, (1994).

13. Resonance Raman study on the Escherichia coli terminal oxidases, cytochrome bo and bd complexes.T. Uno, M. Tsubaki, T. Mogi, Y. Nishimura, and Y. Anraku, Proceedings of the Fourteenth International Conference on Raman Spectroscopy, John Wiley & Sons Ltd., pp. 116-117, (1994).

14. Analysis of the proton pump mechanism of terminal oxidases using FT-IR and EPR spectroscopies, Motonari Tsubaki, Hiroshi Hori, Tatsushi Mogi, and Yashuhiro Anraku, Proceedings of the 20th Annual Meeting of the Japanese Bioenergetics Group(Toyonaka)(in Japanese), pp. 66-67. (1994).

15. Analysis of the proton pump mechanism of terminal oxidases using FT-IR and EPR spectroscopies, Motonari Tsubaki, Proceedings of the 21th Annual Meeting of the Japanese Bioenergetics Group(Nagoya)(in Japanese), pp. 62-63, (1995).

16. cDNA cloning and molecular analysis of the functinally important sites of cytochrome b561 in chromaffin vesicle membranes, Motonari Tsubaki, Masato Nakayama, Eisaku Okuyama, Yoshiyuki Ichikawa,and Hiroshi Hori, The 24th Symposium on Biomolecular Science (Okazki) (in Japanese), pp. 66-67, (1997).

17. Electron transfer reaction from ascorbate to cytochrome b561 in adrenal chromaffin vesicle membranes, Motonari Tsubaki, Tomoko Ichise, Fusako Takeuchi, Hiroshi Hori, Kazuo Kobayashi, and Seiichi Tagawa, The 25th Symposium on Biomolecular Science (Nishinomiya) (in Japanese), pp. 78-79, (1998).

18. Analysis on the electron transfer mechanism of adrenal chromaffin cytochrome b561 and ascorbate using MALDI-TOF-MS technique, Motonari Tsubaki and Fusako Takeuchi, The 26th Symposium on Biomolecular Science (Yokohama) (in Japanese),pp. 54-55, (1999).

19. Structure and function of the electron transport system in the neuroendocrine vesicle membranes, Motonari Tsubaki, Hyogo Science and Technology Association Annual Research Reports 1999 (in Japanese), pp. 33-41, (1999).

20. Analysis of the cytochrome b561-ascorbate electron transfer mechanism using MALDI-TOF-MS technique, Motonari Tsubaki, Fusako Takeuchi, Kazuo Kobayashi, Seiichi Tagawa, The 27th Symposium on Biomolecular Science (Sendai) (in Japanese), pp.44-45, (2000).

21. Cytochrome b561-ascorbate electron transfer mechanism in the neuroendcrine vesicles, Motonari Tsubaki, Fusako Takeuchi, Kazuo Kobayashi, Seiichi Tagawa,and Hirosi Hori, The 28th Symposium on Biomolecular Science (Kanazawa) (in Japanese), pp. 56-57, (2001).

22. Analysis of the neuroendocrine vesicle cytochrome b561-electron transfer system using the reconstituted proteoliposomes, Yumiko Seike, Mariko Nakamura, Fusako Takeuchi, and Motonari Tsubaki, The 29th Symposium on Biomolecular Science (Okazaki) (in Japanese), pp.56-57,(2002).

23. Stopped-flow analysis of the electron transfer reaction between ascorbate and cytochrome b561, Tadakazu Takigami, Fusako Takeuchi, Masashi Nakagawa, Toshiharu Hase, and Motonari Tsubaki, The 30th Symposium on Biomolecular Science (Kyoto) (in Japanese), pp.28-29, (2003).

24. Redox changes of cytochrome b5 upon treatment with diethyl pyrocarbonate, Nobuyuki Nakanishi, Fusako Takeuchi, Hiroshi Hori, and Motonari Tsubaki, The 31th Symposium on Biomolecular Science (Mito) (in Japanese), pp. 57-58 (2004).

25. Interaction of Tail-anchored Proteins with Liposomes in Different Cholesterol Content: Initial Steps for the Fabrication of Artificial Neuroendocrine Vesicles, Jun Hamada, Nobuyuki Nakanishi, Fusako Takeuchi, Sam-Yong Park, and Motonari Tsubaki; Summarized Report of Symposium on System Cell Engineering by Multi-scale Manipulation at MHS2006 & Micro-COE Symposium, pp. 82-87 (2006).

26. "Pulse radiolysis studies in biological systems 1: Physiological roles of ascorbate in the plant transmembrane electron transfer reaction: Reaction mechansim of Zea mays cytochrome b561 with ascorbate and monodehydroascorbate radical", Kobayashi, K., Tagawa, S., Nakanishi, N., Rahman, Md. M., and Tsuaki, M., in "Research Reports of Radiation Laboratories, ISIR", 3-12, (2007).

27. "Roles of Tyr71 and Arg72 in the ascorbate-specific electron transfer reaction of Zea mays cytohrome b561", Rahman, Md. M., Fujito, M., Nakanishi, N., Hase, T., Park, S.-Y., and Tsubaki, M., The 35th Symposium on Biomolecular Science (Hyogo, Akou-gun) (in Japanese), pp. 31-32 (2008).

28."Analyses on the novel function of the cytochrome b561 protein family in Caenorhabditis elegans ", Miura, M., Tsubaki, M., The 37th Symposium on Biomolecular Science (Yamaguchi) (in Japanese), pp. 42-43 (2010).