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. 総説類
75. "ヘムタンパク質のヘム配位子と蛋白の相互作用", 堀洋、鍔木基成, 生物物理、22、151-159, (1982).
76. "赤外分光法によるヘム・銅末端酸化酵素の構造解析", 鍔木基成, 生物物理、35, 107-112, (1995).
77. 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).
78. 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).
79. 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).
80. 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. 著書
81. 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).
82. 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).
83. 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).
84. 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).
85. 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).
86. 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) (in press)
IV. プロシーディング等
87. 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).
88. "ヘモグロビン、ミオグロビンにおけるヘム-配位子結合の共鳴ラマン散乱法による研究：CO, CNの結合を中心として", 鍔木基成、Nai-Teng Yu, R. B. Srivastava, 第 33回タンパク質構造討論会要旨集（大阪）, pp. 41-44, (1982).
89. 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).
90. 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)
91. "共鳴ラマン散乱法によるシトクロムP-450sccの活性中心の構造と機能の研究", 鍔木基成、樋渡敦夫、市川佳幸, 第13回生体分子の構造と機能に関する討論会要旨集（岡崎）, pp.45-46, (1986).
92. "シトクロムP-450 水酸化酵素系活性中心（ヘム）の物理化学的研究 ", 鍔木基成, 内藤記念科学振興財団研究報告集 昭和６１年度版、pp.90-91, (1986).
93. "シトクロムP-450scc(Fe2+-NO)複合体とコレステロール、アドレノドキシンとの相互作用：EPRによる研究", 鍔木基成、樋渡敦夫、市川佳幸、堀洋, 第14回生体分子の構造と機能に関する討論会要旨集（東京）, pp.57-58, (1987).
94. "トロンボキサンＡ合成酵素阻害薬の分子レベルにおける阻害機構：シトクロムP-450としての酵素的性質", 鍔木基成, 持田記念財団研究成果報告集, ４, 153-157, (1988).
95. "大腸菌シトクロムbo複合体とミトコンドリアシトクロム酸化酵素の反応中心の類似性：赤外スペクトルによる解析", 鍔木基成、茂木立志、吉川信也、安楽泰宏, 日本生体エネルギー研究会第１７回討論会要旨集（東京）, pp. 32-33, (1991).
96. "大腸菌シトクロムbo複合体複核反応中心の構造：EPRと赤外スペクトルによる解析", 鍔木基成、吉川信也、堀 洋、茂木立志、安楽泰宏, 日本生体エネルギー研究会第１８回討論会要旨集（東京）, pp. 152-153, (1992).
97. "FT-IRとEPRによる末端酸化酵素プロトンポンプの機構の解明", 鍔木基成, 日本生体エネルギー研究会第１９回討論会要旨集（豊中）, pp. 86-87, (1993).
98. "EPR測定により新たに見出されたシトクロムP450c21によるステロイドオキシダーゼ活性", 鍔木基成、森本幸嗣、富田修平、三浦成敏、市川佳幸、桝屋太志、堀洋, 第21回生体分子の構造と機能に関する討論会要旨集（東京）, pp. 13-14, (1994).
99. 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).
100. "FT-IR とEPRによる末端酸化酵素プロトンポンプ機構の解明", 鍔木基成、堀洋、茂木立志、安楽泰宏, 日本生体エネルギー研究会第２０回討論会要旨集（豊中）, pp. 66-67. (1994).
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102. "クロマフィン小胞膜に存在するシトクロムb561のcDNAクローニングと機能活性部位の解析", 鍔木基成、中山雅登、奥山英策、市川佳幸、堀 洋, 第24回生体分子科学討論会要旨集（岡崎）, pp. 66-67, (1997).
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104. "MALDI-TOF-MS法による副腎クロマフィン小胞由来チトクロムb561とアスコルビン酸との電子伝達機構の解析", 鍔木基成、武内総子, 第26回生体分子科学討論会要旨集（横浜）, pp. 54-55, (1999).
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110. "Diethyl pyrocarbonate処理に伴うcytochrome b5のredox変化"
中西伸行、武内総子、堀 洋、鍔木基成
第31回生体分子科学討論会（水戸、茨城），pp.57-58 (2004）