業績

1. S. Tuzi, S. Yamaguchi, A. Naito, R. Needleman, J. K. Lanyi, H. Saitô,
  Conformation and Dynamics of [3-13C] Ala-Labeled Bacteriorhodopsin and
  Bacterioopsin, Induced by Interaction with Retinal and Its Analogs, As Studied by
  13C Nuclear Magnetic Resonance, Biochemistry, 35, 7520-7527, (1996)

2. S. Yamaguchi, S. Tuzi, T. Seki, M. Tanio, J. K. Lanyi, R. Needleman, A. Naito,
  H. Saitô,
  Stability of the C-Terminal -Helical Domain of Bacteriorhodopsin. That protrudes
  the Membrane Surface, as Studied by High-Resolution Solid-State NMR,
  J.Biochem., 123, 78-86, (1998)

3. H. Saitô, S. Tuzi, S. Yamaguchi, M. Tanio, S. Kimura, M. Kamihira, K. Nishimura,
  A. Naito,
  Conformation and Dynamics of Membrane Proteins and Biologically Active Peptide
  as Studied by High-resolution Solid State 13C NMR, J. Mol. Struct. , 441, 137-148,
  (1998)

4. S. Tuzi, S. Yamaguchi, M. Tanio, H. Konishi, S. Inoue, A. Naito, R. Needleman,
  J. K. anyi, H. Saitô
  Location of Cation-Binding Site in the Loop between Helices F and G of
  Bacteriorhodopsin as Studied by 13C NMR, Biophys. J., 76, 1523-1531,(1999)

5. M. Tanio, S. Tuzi, S. Yamaguchi, H. Konishi, A. Naito, R. Needleman, J. K. Lanyi,
  H. Saitô,
  Evidence of Local conformational fluctuations and changes in bacteriorhodopsin,
  dependent on lipids, detergents and trimeric structure, as studied by 13C NMR,
  Biochim. Biophys. Acta-Biomembrane, 1375, 84-92, (1999)

6. M. Tanio, S. Tuzi, S. Yamaguchi, R. Kawaminami, A. Naito, R. Needleman,
  J. K. Lanyi, H. Saitô,
  Conformational Change of Bacteriorhodopsin along the Proton-Conduction Chain
  as Studied with 13C NMR of [3-13C]Ala-Labeled Protein: Arg82 May Function as
  an Information Mediator, Biophys. J., 77, 1577-1584, (1999)

7. Y. Kawase, M. Tanio, A. Kira, S. Yamaguchi, S. Tuzi, A. Naito, M. Kataoka,
  J. K. Lanyi, R. Needleman, H. Saitô,
  Alteration of Conformation and Dynamics of Bacteriorhodopsin by Protonation of
  Asp 85 and Deprotonation of Schiff Base as Studied by 13C NMR,
  Biochemistry, 39, 14472-14480, (2000)

8. S. Yamaguchi, S. Tuzi, M. Tanio, A. Naito, J. K. Lanyi, R. Needleman, H. Saitô,
  Irreversible conformational Change of Bacteriorho-opsin Induced by Binding of
  Retinal during Its Reconstitution to Bacteriorhodopsin, as Studied by 13C NMR,
  J.Biochem., 127, 861-869, (2000)

9. D. Huster, S. Yamaguchi, M. Hong,
  Efficient β-sheet Identification in Protein by Solid-State NMR
  J. Am. Chem. Soc., 122, 11320-11327, (2000)

10. S. Yamaguchi, K. Yonebayashi, H. Konishi, S. Tuzi, A. Naito, J.K. Lanyi ,
  R. Needleman, H. Saitô,
  Cytoplasmic surface structure of bacteriorhodopsin consisting of interhelical
  loops and C-terminal alpha helix, modified by a variety of environmental factors
  as studied by 13C NMR, Eur. J. Biochem., 268, 2218-2228, (2001)

11. S. Yamaguchi, S. Tuzi, K. Yonebayashi, A. Naito, R. Needleman, J. K. Lanyi,
  H. Saitô,
  Surface Dynamics of Bacteriorhodopsin as Revealed by 13C NMR Studies on
  [13C]Ala-labeled Proteins: Determination of Millisecond or Microsecond Motions
  in Interhelical Loops and C-terminal α-helix, J. Biochem., 129, 373-382, (2001)

12. M. Hong and S. Yamaguchi
  Sensitivity-Enhanced Static 15N NMR of Solids by 1H Indirect Detection,
  J.Magn. Reson.,150, 43-48, (2001)

13. S. Yamaguchi, D. Huster, B.F. Tack, W. Kearney, A. Waring, R.I. Lehrer, M. Hong
  Orientation and Dynamics of an Antimicrobial Peptide in the Lipid Bilayer by
  Solid-State NMR, Biophys. J., 81, 2203-2214, (2001)

14. H. Saitô, T. Tsuchida, K. Ogawa, T. Arakawa, S. Yamaguchi, S. Tuzi
  Residue-specific millisecond to microsecond fluctions in bacteriorhodopsin
  induced by disrupted or disorganized two-dimensional crystalline lattice,
  through modified lipid-helix and helix-helix interactions, as revealed by 13C NMR,
  Biochimica et Biophysica Acta - Biomembrane, 1565, 97-106, (2002)

15. H. Saitô, R. Kawaminami, M. Tanio, T.Arakawa, S.Yamaguchi, S.Tuzi
  Dynamic Aspect of Bacteriorhodopsin as Viewed from 13C NMR : Conformational
  Elucidation, Surface Dynamics and Information Transfer from the Surface to
  Inner Residues, Spectroscopy, 16, 107-120, (2002)

16. S. Yamaguchi, T. Hong, A. Waring, R.I. Lehrer, M. Hong
  Solid-State NMR Investigations of Peptide-Lipid Interaction and Orientation of
  a b-Sheet Antimicrobial Peptide, Protegrin, Biochemistry, 41, 9852-9862, (2002)

17. X. Yao, S. Yamaguchi, M. Hong
  Ca chemical shift tensors in helical peptides by dipolar-modulated chemical shift
  Recoupling NMR, J Biomol NMR., 24, 51-62, (2002)

18. H. Saitô, S. Yamaguchi, S. Tuzi,
  Dynamic Structure of Bacteriorhodopsin Reveales by 13C Solid State NMR,
  Journal of Photoscience, 9, 110-113, (2002)

19. S. Yamaguchi and M. Hong,
  Determination of Membrane Peptide Orientation by 1H-InDetected 2H NMR
  Spectroscopy, J. Magn.Reson., 155, 244-250, (2002)

20. K. Yonebayashi, S. Yamaguchi, S. Tuzi, H. Saitô,
  Cytoplasmic Surface Structures of Bacteriorhodopsin Modifed by Site-directed
  Mutationss and Cation-binding as Revealed by 13C NMR,
  Europian Biophys. J., 32, 1-11, (2003)

21. T. Arakawa, K. Shimono, S. Yamaguchi, S. Tuzi, Y. Sudo, N. Kamo, H. Saitô,
  Dynamic Structure of pharaonis phoborhodopsin ( Sensory Rhodopsin II) and
  Complex with a Cognate Trancated Transducer as Revealed by Site-directed 13C
  Solid-state NMR, FEBS Lett., 536, 237-240, (2003)

22. P. Barré, S. Yamaguchi, H. Saitô, D. Huster
  Backbone dynamics of bacteriorhodopsin as studied by 13C solid-state NMR
  spectroscopy, Europian Biophys. J., 32, 578-584, (2003)

23. S. Tuzi, N. Uekama, M. Okada, S. Yamaguchi, H. Saitô, H. Yagisawa
  Structure and dynamics of the phospholipase C-delta 1 PH domain located at the
  lipid bilayer surface, J. Biol. Chem., 278, 28019-28025, (2003)

24. JJ. Buffy, T. Hong, S. Yamaguchi, AJ. Waring, RI. Lehrer, M. Hong.
  Solid-state NMR investigation of the depth of insertion of protegrin-1 in lipid
  bilayers Using paramagnetic Mn2+, Biophys J., 85, 2363-2373, (2003)

25. H. Saitô, K. Yamamoto, S. Tuzi, S Yamaguchi*
  Backbone Dynamics of Membrane Proteins in Lipid Bilayers: The Effect of Two
  Dimensional Array Formation as Revealed by Site-directed Solid-state 13C NMR
  Studies on [3-13C]Ala- and [1-13C]Val-labeled Bacteriorhodopsin,
  Biochimica et Biophysica Acta - Biomembrane, 1616, 127-136, (2003)

26. H. Saitô, S. Yamaguchi, H. Okuda, A. Shiraishi, S. Tuzi
  Dynamic Structure of Bacteriorhodopsin as a Typical Membrane Protein as
  Revealed by Site-directed Solid-state 13C NMR, Solid State NMR, 25, 5-14,
  (2004)

27. H. Saitô, S. Yamaguchi, K. Ogawa, S. Tuzi, M. Marquez, C. Sanz, E. Padros
  Glutamic Acid residues of bacteriorhodopsin at the extracellular surface as
  determinants for Conformation and dynamics as revealed by site-directed
  solid-state 13C NMR, Biophys J., 86, 1673-1681, (2004)

28. S. Yamaguchi*, J.U. Bowie , S. Tuzi, H. Saitô 
  Secondary Structure and Backbone Dynamics of Escherichia coli Diacylglycerol
  Kinase, as Revealed By Site-directed Solid-state 13C NMR,
  Biochimica et Biophysica Acta–Proteis and Proteomics, 1698, 97-105, (2004)

29. H. Saitô, J. Mikami, S. Yamaguchi, M. Tanio, A. Kira, T. Arakawa, K. Yamamoto,
  S. Tuzi
  Site-directed 13C solid-state NMR studies on membrane proteins: strategy and
  goals toward revealing conformation and dynamics as illustrated for
  bacteriorhodopsin labeled with [1-13C]amino acid residues,
  Magn Reson Chem., 42, 218-230, (2004)

30. S. Yamaguchi, K. Shimono, Y. Sudo, S. Tuzi, A. Naito, N. Kamo, H. Saitô
  Conformation and Dynamics of [3-13C]Ala,- [1-13C]Val- labeled Truncated
  pharaonis Transducer, pHtrII(1-159) as Revealed by Site-directed 13C Solid-state
  NMR: Changes Due to Association with Phoborhodopsin (Sensory Rhodopsin II)
  Biophys J., 86, 3131-3140, (2004)

31. I. Kawamura, Y. Degawa, S. Yamaguchi, K. Nishimura, S. Tuzi, H. Saitô, A. Naito
  Pressure-induced isomerization of retinal on bacteriorhodopsin as disclosed by
  fast magic angle spinning NMR, Photochem Photobiol., 83, 346-350, (2007)

32. I. Kawamura, Y. Ikeda, Y. Sudo, M. Iwamoto, K. Shimono, S. Yamaguchi, S. Tuzi,
  H. Saitô, N. Kamo, A. Naito.
  Participation of the surface structure of Phara phoborhodopsin, ppR and its
  A149and A149V mutants, consisting of the C-terminal alpha-helix and E-F loop,
  in the complex-formation with the cognate transducer pHtrII, as revealed by
  site-directed 13C solid-state NMR, Photochem Photobiol., 83, 339-345, (2007)

33. H. Sugiyama, R. Nakatsubo, S. Yamaguchi, T. Ogura , K. Shinzawa-Itoh,
  S. Yoshikawa
  Resonance Raman spectra of the FMN of the bovine heart NADH: ubiquinone
  oxidoreductase, the largest membrane protein in the mitochondrial respiratory
  system, J Bioenerg Biomembr., 39, 145-148, (2007)

34. I. Kawamura, H. Yoshida, Y. Ikeda, S. Yamaguchi, S. Tuzi, H. Saitô, N. Kamo,
  A. Naito.
  Dynamics Change of Phoborhodopsin and Transducer by Activation: Study Using
  D75N Mutant of the Receptor by Site-directed Solid-state 13C NMR, Photochem
  Photobiol., 84, 291-230, (2008)

35. K. Ikemura, M. Mukai, H. Shimada, T. Tsukihara, S. Yamaguchi,
  K. Shinzawa-Itoh, S. Yoshikawa,T. Ogura
  Red-Excitation Resonance Raman Analysis of the nFe=O Mode of
  Ferryl-Oxo Hemoproteins, J. Am. Chem. Soc., 130, 14384-14385, (2008)

36. I. Kawamura, J. Tanabe, M. Ohmine, S. Yamaguchi, S. Tuzi, A. Naito
  Participation of the BC loop in the correct folding of bacteriorhodopsin as
  revealed by solid-state NMR, Photochemistry and Photobiology, 85, 624-630,
  (2009)

37. J.G. Liu, T. Ohta, S. Yamaguchi, T. Ogura, S. Sakamoto, Y. Maeda, Y. Naruta
  Spectroscopic Characterization of a Hydroperoxo-Heme Intermediate:
  Conversion of a Side-On Peroxo to an End-On Hydroperoxo,
  Angewandte Chemie International Edition, 48, 9262-9267,(2009) ,selected VIP
  (Very Important Paper)

38. N. Uekama, T. Aoki, T. Maruoka, S. Kurisu, A. Hatakeyama, S. Yamaguchi,
  M. Okada, H. Yagisawa, K. Nishimura, S. Tuzi
  Influence of Membrane Curvature on the Structure of the Membrane-Associated
  Pleckstrin Homology Domain of Phospholipase C-d1, Biochimica et Biophysica
  Acta - Biomembrane, 1788, 2575-2583, (2009)

39. T. Tano, M.Z. Ertem, S. Yamaguchi, A. Kunishita, H. Sugimoto, N. Fujieda,
  T. Ogura, C.J. Cramer, S. Itoh
  Reactivity of copper(II)-alkylperoxo complexes,
  Dalton Transactions, 40, 10326-10336, (2011)

40. M. Murakami, D. Hong, T. Suenobu, S. Yamaguchi, T. Ogura, S. Fukuzumi
  Catalytic mechanism of water oxidation with single-site
  ruthenium-heteropolytungstate complexes,
  J. Am. Chem. Soc.,133, 11605-11613, (2011)

41. N.Tokiuda, K.Kawai, YH. Lee, T. Ikegami, S. Yamaguchi, H. Yagisawa, Y. Fukui,
  S. Tuzi.
  Membrane-induced alteration of the secondary structure in the
  SWAP-70 pleckstrin homology domain, J Biochem., 151, 391-401, (2012)

42. I. Kawamura, S. Yamaguchi, H. Nishikawa, K. Tajima, M. Horigoe, S. tuzi,
  H. Saito, A. Naito
  Change in local dynamics of bacteriorhodopsin with retinal isomerization under
  pressure as studied by fast magic angle spinning NMR,
  Polymer Journal, 44, 863-867, (2012)

43. M. Kubo, S. Nakashima, S. Yamaguchi, T. Ogura, M. Mochizuki, J. Kang,
  M. Tateno, K. Shinzawa-Itoh,K. Kato, S. Yoshikawa.
  Effective pumping proton collection facilitated by a copper site (CuB) of bovine
  heart cytochrome coxidase, revealed by a newly developed time-resolved
  infrared system, J Biol Chem. 288, 30259-30269, (2013)

2)プロシーディングス

1. S. Yamaguchi, S. Tuzi, R. Needleman, J. K. Lanyi, A. Naito, H. Saito
  C-terminal a-helical Domain of Bacteriorhodopsin at the Membrane Surface
  Analyzed by Magnetic Resonance/Spectroscopy in Food Science:
  Proceedings of The International Workshop on Applications of Magnetic
  Resonance and Other Spectroscopic Techniques to Food Science, ed. By H Saito
  and G.A. Webb, pp. 131-134 (1997)

2. S. Tuzi, S. Yamaguchi, M. Tanio, Y. Kawase, J. K. Lanyi, R. Needleman, A. Naito,
  and H. Saito
  Conformation and BackboneDynamics of Bacteriorhodopsin at Ambient
  Temperature as Revealed by High-Resolution Solid-state 13C NMR, Proceedings of
  the Joint 29th AMPERE-13th ISMAR International Conference, ed. by
  D. Ziessow, W. Lubitz and F. Lendzian, vil.I, pp. 454-455, (1998)

3)総説

1. H. Saitô, S. Tuzi, S. Yamaguchi, M. Tanio, A. Naito
  Conformation and Backbone Dynamics of Bacteriorhodopsin Revealed by
  13C NMR,
  Biochimica et Biophysica Acta- Bioenergetics, 1460, 39-48, (2000)

2. H. Saitô, Y. Kawase, A. Kira, K. Yamamoto, M. Tanio, S. Yamaguchi, S. Tuzi,
  A. Naito.
  Surface and dynamic structures of bacteriorhodopsin in a 2D crystal, a distorted
  or disrupted lattice, as revealed by site-directed solid-state 13C NMR,
  Photochem Photobiol., 83, 253-262, (2007)