$\require{mediawiki-texvc}$

연합인증

연합인증 가입 기관의 연구자들은 소속기관의 인증정보(ID와 암호)를 이용해 다른 대학, 연구기관, 서비스 공급자의 다양한 온라인 자원과 연구 데이터를 이용할 수 있습니다.

이는 여행자가 자국에서 발행 받은 여권으로 세계 각국을 자유롭게 여행할 수 있는 것과 같습니다.

연합인증으로 이용이 가능한 서비스는 NTIS, DataON, Edison, Kafe, Webinar 등이 있습니다.

한번의 인증절차만으로 연합인증 가입 서비스에 추가 로그인 없이 이용이 가능합니다.

다만, 연합인증을 위해서는 최초 1회만 인증 절차가 필요합니다. (회원이 아닐 경우 회원 가입이 필요합니다.)

연합인증 절차는 다음과 같습니다.

최초이용시에는
ScienceON에 로그인 → 연합인증 서비스 접속 → 로그인 (본인 확인 또는 회원가입) → 서비스 이용

그 이후에는
ScienceON 로그인 → 연합인증 서비스 접속 → 서비스 이용

연합인증을 활용하시면 KISTI가 제공하는 다양한 서비스를 편리하게 이용하실 수 있습니다.

Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins

Photochemical & photobiological sciences : an international journal, v.8 no.11, 2009년, pp.1517 - 1528  

Radu, Ionela (Bielefeld University, Department of Chemistry, Biophysical Chemistry) ,  Schleeger, Michael (Bielefeld University, Department of Chemistry, Biophysical Chemistry) ,  Bolwien, Carsten (Fraunhofer Institute for Physical Measurement Techniques IPM) ,  Heberle, Joachim (Bielefeld University, Department of Chemistry, Biophysical Chemistry)

Abstract AI-Helper 아이콘AI-Helper

The introduction of time-resolved Fourier transform infrared (FT-IR) spectroscopy to biochemistry opened the possibility of monitoring the catalytic mechanism of proteins along their reaction pathways. The infrared approach is very fruitful, particularly in the application to membrane proteins where...

참고문헌 (90)

  1. Rev. Sci. Instrum. C J Manning 62 1219 1991 10.1063/1.1142003 C. J. Manning, R. A. Palmer, J. L. Chao, Step-Scan Fourier-Transform Infrared Spectrometer, Rev. Sci. Instrum., 1991, 62, 1219-1229. 

  2. Appl. Spectrosc. W Uhmann 45 390 1991 10.1366/0003702914337128 W. Uhmann, A. Becker, C. Taran, F. Siebert, Time-Resolved FT-IR Absorption Spectroscopy Using a Step-Scan Interferometer, Appl. Spectrosc., 1991, 45, 390-397. 

  3. P R Griffiths 1986 Fourier transform infrared spectrometry P. R. Griffiths and J. A. de Haseth, in Fourier transform infrared spectrometry, John Wiley & Sons Inc., New York, 1986. 

  4. Appl. Spectrosc. P Y Chen 51 580 1997 10.1366/0003702971940648 P. Y. Chen, R. A. Palmer, Ten-nanosecond step-scan FT-IR absorption difference time-resolved spectroscopy: Applications to excited states of transition metal complexes, Appl. Spectrosc., 1997, 51, 580-583. 

  5. Appl. Spectrosc. R Rammelsberg 51 558 1997 10.1366/0003702971940585 R. Rammelsberg, B. Heßling, H. Chorongiewski, K. Gerwert, Molecular Reaction Mechanism of Proteins Monitored by Nanosecond Step-Scan FT-IR Difference Spectroscopy, Appl. Spectrosc., 1997, 51, 558-562. 

  6. FEBS Lett. R M Nyquist 505 63 2001 10.1016/S0014-5793(01)02769-7 R. M. Nyquist, D. Heitbrink, C. Bolwien, T. A. Wells, R. B. Gennis, J. Heberle, Perfusion-induced redox differences in cytochrome c oxidase: ATR/FT-IR spectroscopy, FEBS Lett., 2001, 505, 63-67. 

  7. Appl. Spectrosc. J Heberle 50 588 1996 10.1366/0003702963905907 J. Heberle, C. Zscherp, ATR/FT-IR difference spectroscopy of biological matter with microsecond time resolution, Appl. Spectrosc., 1996, 50, 588-596. 

  8. J. Electron Spectrosc. Relat. Phenom. M Osawa 64-65 371 1993 10.1016/0368-2048(93)80099-8 M. Osawa, K. Ataka, K. Yoshii, T. Yotsuyanagi, Surface-Enhanced Infrared Atr Spectroscopy for In situ Studies of Electrode-Electrolyte Interfaces, J. Electron Spectrosc. Relat. Phenom., 1993, 64-65, 371-379. au9_M. Osawa, Surface-enhanced infrared absorption spectroscopy, in Handbook of Vibrational Spectroscopy, ed. J. M. Chalmers and P. R. Griffiths, Wiley, Chichester, 2002, pp. 785-799. 

  9. Appl. Spectrosc. R F Aroca 58 324A 2004 10.1366/0003702042475420 R. F. Aroca, D. J. Ross, C. Domingo, Surface-enhanced infrared spectroscopy, Appl. Spectrosc., 2004, 58, 324A-338A. 

  10. J. Am. Chem. Soc. K Ataka 126 16199 2004 10.1021/ja045951h K. Ataka, F. Giess, W. Knoll, R. Naumann, S. Haber-Pohlmeier, B. Richter, J. Heberle, Oriented Attachment and Membrane Reconstitution of His-Tagged Cytochrome c Oxidase to a Gold Electrode: In Situ Monitoring by Surface-Enhanced Infrared Absorption Spectroscopy, J. Am. Chem. Soc., 2004, 126, 16199-16206. 

  11. J. Am. Chem. Soc. K Ataka 125 4986 2003 10.1021/ja0346532 K. Ataka, J. Heberle, Electrochemically Induced Surface-Enhanced Infrared Difference Absorption (SEIDA) Spectroscopy of a Protein Monolayer, J. Am. Chem. Soc., 2003, 125, 4986-4987. au13_B. Selinsky, Membrane Protein Protocols: Expression, Purification, and Crystallization, Humana Press, Totowa, NJ, 2003. 

  12. Curr. Opin. Struct. Biol. C Hunte 12 503 2002 10.1016/S0959-440X(02)00354-8 C. Hunte, H. Michel, Crystallisation of membrane proteins mediated by antibody fragments, Curr. Opin. Struct. Biol., 2002, 12, 503-508. 

  13. Curr. Opin. Struct. Biol. C Ostermeier 7 697 1997 10.1016/S0959-440X(97)80080-2 C. Ostermeier, H. Michel, Crystallization of membrane proteins, Curr. Opin. Struct. Biol., 1997, 7, 697-701. 

  14. Methods Enzymol. P Nollert 343 183 2002 10.1016/S0076-6879(02)43135-7 P. Nollert, J. Navarro, E. M. Landau, Crystallization of membrane proteins in cubo, Methods Enzymol., 2002, 343, 183-199. 

  15. Biophys. J. R H Lozier 15 955 1975 10.1016/S0006-3495(75)85875-9 R. H. Lozier, R. A. Bogomolni, W. Stoeckenius, Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium, Biophys. J., 1975, 15, 955-962. 

  16. Biophys. J. I Chizhov 71 2329 1996 10.1016/S0006-3495(96)79475-4 I. Chizhov, D. S. Chernavskii, M. Engelhard, K. H. Mueller, B. V. Zubov, B. Hess, Spectrally silent transitions in the bacteriorhodopsin photocycle, Biophys. J., 1996, 71, 2329-2345. 

  17. Appl. Spectrosc. O Weidlich 47 1394 1993 10.1366/0003702934067351 O. Weidlich, F. Siebert, Time Resolved Step-Scan FTIR Investigations of the Transition from KL to L in the Bacteriorhodpsin Photocycle: Identification of Chromophore Twists by Assigning Hydrogen-Out-Of-Plane (HOOP) Bending Vibrations, Appl. Spectrosc., 1993, 47, 1394-1400. 

  18. Biophys. J. C Rödig 76 2687 1999 10.1016/S0006-3495(99)77421-7 C. Rödig, I. Chizhov, O. Weidlich, F. Siebert, Time-Resolved Step-Scan Fourier Transform Infrared Spectroscopy Reveals Differences between Early and Late M Intermediates of Bacteriorhodopsin, Biophys. J., 1999, 76, 2687-2701. 

  19. J. Phys. Chem. W Hage 100 16026 1996 10.1021/jp9614198 W. Hage, M. Kim, H. Frei, R. A. Mathies, Protein dynamics in the bacteriorhodopsin photocycle: A nanosecond step-scan FTIR investigation of the KL to L transition, J. Phys. Chem., 1996, 100, 16026-16033. 

  20. Biophys. J. J Sasaki 68 2073 1995 10.1016/S0006-3495(95)80386-3 J. Sasaki, T. Yuzawa, H. Kandori, A. Maeda, H. Hamaguchi, Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle, Biophys. J., 1995, 68, 2073-2080. 

  21. J. Phys. Chem. B A K Dioumaev 101 1655 1997 10.1021/jp961512w A. K. Dioumaev, M. S. Braiman, Two Bathointermediates of the Bacteriorhodopsin Photocycle, Distinguished by Nanosecond Time-Resolved FTIR Spectroscopy at Room Temperature, J. Phys. Chem. B, 1997, 101, 1655-1662. 

  22. J. Phys. Chem. B C Zscherp 101 10542 1997 10.1021/jp971047i C. Zscherp, J. Heberle, Infrared difference spectra of the intermediates L, M, N, and O of the bacteriorhodopsin photoreaction obtained by time-resolved attenuated total reflection spectroscopy, J. Phys. Chem. B, 1997, 101, 10542-10547. 

  23. Biochemistry M Engelhard 24 400 1985 10.1021/bi00323a024 M. Engelhard, K. Gerwert, B. Hess, W. Kreutz, F. Siebert, Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane, Biochemistry, 1985, 24, 400-407. 

  24. Isr. J. Chem. A Maeda 35 387 1995 10.1002/ijch.199500038 A. Maeda, Application of FTIR spectroscopy to the structural study on the function of bacteriorhodopsin, Isr. J. Chem., 1995, 35, 387-400. 

  25. Biophys. Chem. J Heberle 85 229 2000 10.1016/S0301-4622(99)00154-4 J. Heberle, J. Fitter, H. J. Sass, G. Büldt, Bacteriorhodopsin: the functional details of a molecular machine are being resolved, Biophys. Chem., 2000, 85, 229-248. 

  26. Biochim. Biophys. Acta, Bioenerg. J Heberle 1458 135 2000 10.1016/S0005-2728(00)00064-5 J. Heberle, Proton transfer reactions across bacteriorhodopsin and along the membrane, Biochim. Biophys. Acta, Bioenerg., 2000, 1458, 135-147. 

  27. Biochemistry (Moscow) A K Dioumaev 66 1269 2001 10.1023/A:1013135419529 A. K. Dioumaev, Infrared methods for monitoring the protonation state of carboxylic amino acids in the photocycle of bacteriorhodopsin, Biochemistry (Moscow), 2001, 66, 1269-1276. 

  28. Biophys. J. F Garczarek 87 2676 2004 10.1529/biophysj.104.046433 F. Garczarek, J. Wang, M. A. El-Sayed, K. Gerwert, The Assignment of the Different Infrared Continuum Absorbance Changes Observed in the 3000-1800-cm−1 Region During the Bacteriorhodopsin Photocycle, Biophys. J., 2004, 87, 2676-1682. 

  29. Nature F Garczarek 439 109 2006 10.1038/nature04231 F. Garczarek, K. Gerwert, Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy, Nature, 2006, 439, 109-112. 

  30. Biochemistry R Rammelsberg 37 5001 1998 10.1021/bi971701k R. Rammelsberg, G. Huhn, M. Lübben, K. Gerwert, Bacteriorhodopsin’s intramolecular proton-release pathway consists of a hydrogen-bonded network, Biochemistry, 1998, 37, 5001-5009. 

  31. Biophys. J. J Heberle 87 2105 2004 10.1529/biophysj.104.050054 J. Heberle, A local area network of protonated water molecules, Biophys. J., 2004, 87, 2105-2106. 

  32. Proc. Natl. Acad. Sci. U. S. A. G Mathias 104 6980 2007 10.1073/pnas.0609229104 G. Mathias, D. Marx, Structures and spectral signatures of protonated water networks in bacteriorhodopsin, Proc. Natl. Acad. Sci. U. S. A., 2007, 104, 6980-6985. 

  33. Photosynth. Res. J Breton 55 301 1998 10.1023/A:1005972514425 J. Breton, E. Nabedryk, Proton uptake upon quinone reduction in bacterial reaction centers: IR signature and possible participation of a highly polarizable hydrogen bond network, Photosynth. Res., 1998, 55, 301-307. 

  34. Biochemistry J E Morgan 46 2787 2007 10.1021/bi0616596 J. E. Morgan, A. S. Vakkasoglu, R. B. Gennis, A. Maeda, Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy, Biochemistry, 2007, 46, 2787-2796. 

  35. Biochemistry J E Morgan 47 11598 2008 10.1021/bi801405v J. E. Morgan, A. S. Vakkasoglu, J. Lugtenburg, R. B. Gennis, A. Maeda, Structural changes due to the deprotonation of the proton release group in the M-photointermediate of bacteriorhodopsin as revealed by time-resolved FTIR spectroscopy, Biochemistry, 2008, 47, 11598-11605. 

  36. J. Am. Chem. Soc. V A Lorenz-Fonfria 131 5891 2009 10.1021/ja900334c V. A. Lorenz-Fonfria, H. Kandori, Spectroscopic and kinetic evidence on how bacteriorhodopsin accomplishes vectorial proton transport under functional conditions, J. Am. Chem. Soc., 2009, 131, 5891-5901. 

  37. Proc. Natl. Acad. Sci. U. S. A. C Zscherp 96 5498 1999 10.1073/pnas.96.10.5498 C. Zscherp, R. Schlesinger, J. Tittor, D. Oesterhelt, J. Heberle, In situ determination of transient p Ka changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy, Proc. Natl. Acad. Sci. U. S. A., 1999, 96, 5498-5503. 

  38. Biochemistry J Riesle 35 6635 1996 10.1021/bi9600456 J. Riesle, D. Oesterhelt, N. A. Dencher, J. Heberle, D38 is an essential part of the proton translocation pathway in bacteriorhodopsin, Biochemistry, 1996, 35, 6635-6643. 

  39. J. Mol. Biol. H Luecke 291 899 1999 10.1006/jmbi.1999.3027 H. Luecke, B. Schobert, H. T. Richter, J. P. Cartailler, J. K. Lanyi, Structure of bacteriorhodopsin at 1.55 Å resolution, J. Mol. Biol., 1999, 291, 899-911. 

  40. J. Mol. Biol. J Heberle 281 587 1998 10.1006/jmbi.1998.1970 J. Heberle, G. Büldt, E. Koglin, J. P. Rosenbusch, E. M. Landau, Assessing the functionality of a membrane protein in a three-dimensional crystal, J. Mol. Biol., 1998, 281, 587-592. 

  41. Biophys. J. R Efremov 91 1441 2006 10.1529/biophysj.106.083345 R. Efremov, V. I. Gordeliy, J. Heberle, G. Büldt, Time-resolved microspectroscopy on a single crystal of bacteriorhodopsin reveals lattice-induced differences in the photocycle kinetics, Biophys. J., 2006, 91, 1441-1451. 

  42. Biochemistry B Scharf 33 6387 1994 10.1021/bi00187a002 B. Scharf, M. Engelhard, Blue halorhodopsin from Natronobacterium pharaonis: wavelength regulation by anions, Biochemistry, 1994, 33, 6387-6393. 

  43. Biochemistry G Varo 35 6604 1996 10.1021/bi9601159 G. Varo, L. S. Brown, R. Needleman, J. K. Lanyi, Proton transport by halorhodopsin, Biochemistry, 1996, 35, 6604-6611. 

  44. Biochemistry S Gerscher 36 11012 1997 10.1021/bi970722b S. Gerscher, M. Mylrajan, P. Hildebrandt, M. H. Baron, R. Muller, M. Engelhard, Chromophore-anion interactions in halorhodopsin from Natronobacterium pharaonis probed by time-resolved resonance Raman spectroscopy, Biochemistry, 1997, 36, 11012-11020. 

  45. FEBS Lett. I V Kalaidzidis 427 59 1998 10.1016/S0014-5793(98)00394-9 I. V. Kalaidzidis, Y. L. Kalaidzidis, A. D. Kaulen, Flash-induced voltage changes in halorhodopsin from Natronobacterium pharaonis, FEBS Lett., 1998, 427, 59-63. 

  46. Science M Kolbe 288 1390 2000 10.1126/science.288.5470.1390 M. Kolbe, H. Besir, L. O. Essen, D. Oesterhelt, Structure of the light-driven chloride pump halorhodopsin at 1.8 Å resolution, Science, 2000, 288, 1390-1396. 

  47. Photochem. Photobiol. A K Dioumaev 66 755 1997 10.1111/j.1751-1097.1997.tb03220.x A. K. Dioumaev, M. S. Braiman, Nano-and microsecond time-resolved FTIR spectroscopy of the halorhodopsin photocycle, Photochem. Photobiol., 1997, 66, 755-763. 

  48. Biophys. J. M S Hutson 80 1452 2001 10.1016/S0006-3495(01)76117-6 M. S. Hutson, S. V. Shilov, R. Krebs, M. S. Braiman, Halide dependence of the halorhodopsin photocycle as measured by time-resolved infrared spectra, Biophys. J., 2001, 80, 1452-1465. 

  49. Biophys. Chem. Q M Mitrovich 56 121 1995 10.1016/0301-4622(95)00023-Q Q. M. Mitrovich, K. G. Victor, M. S. Braiman, Differences between the photocycles of halorhodopsin and the acid purple form of bacteriorhodopsin analyzed with millisecond time-resolved FTIR spectroscopy, Biophys. Chem., 1995, 56, 121-127. 

  50. Biophys. J. C Hackmann 81 394 2001 10.1016/S0006-3495(01)75708-6 C. Hackmann, J. Guijarro, I. Chizhov, M. Engelhard, C. Rödig, F. Siebert, Static and time-resolved step-scan Fourier transform infrared investigations of the photoreaction of halorhodopsin from Natronobacterium pharaonis: consequences for models of the anion translocation mechanism, Biophys. J., 2001, 81, 394-406. 

  51. Proc. Natl. Acad. Sci. U. S. A. A Royant 98 10131 2001 10.1073/pnas.181203898 A. Royant, P. Nollert, K. Edman, R. Neutze, E. M. Landau, E. Pebay-Peyroula, J. Navarro, X-ray structure of sensory rhodopsin II at 2.1-A resolution, Proc. Natl. Acad. Sci. U. S. A., 2001, 98, 10131-10136. 

  52. Science H Luecke 293 1499 2001 10.1126/science.1062977 H. Luecke, B. Schobert, J. K. Lanyi, E. N. Spudich, J. L. Spudich, Crystal Structure of Sensory Rhodopsin II at 2.4 A: Insights into Color Tuning and Transducer Interaction, Science, 2001, 293, 1499-1503. 

  53. Biophys. J. M Hein 84 1208 2003 10.1016/S0006-3495(03)74935-2 M. Hein, A. A. Wegener, M. Engelhard, F. Siebert, Time-Resolved FTIR Studies of Sensory Rhodopsin II (NpSRII) from Natronobacterium pharaonis: Implications for Proton Transport and Receptor Activation, Biophys. J., 2003, 84, 1208-1217. 

  54. Annu. Rev. Cell Dev. Biol. J L Spudich 16 365 2000 10.1146/annurev.cellbio.16.1.365 J. L. Spudich, C. S. Yang, K. H. Jung, E. N. Spudich, Retinyldene Proteins: Structure and function from Archea to Humans, Annu. Rev. Cell Dev. Biol., 2000, 16, 365-392. 

  55. Results Probl. Cell Differ. J P Klare 45 73 2008 10.1007/400_2007_041 J. P. Klare, I. Chizhov, M. Engelhard, Microbial Rhodopsins: Scaffolds for Ion Pumps, Channels, and Sensors, Results Probl. Cell Differ., 2008, 45, 73-122. 

  56. J. Mol. Biol. T Friedrich 321 821 2002 10.1016/S0022-2836(02)00696-4 T. Friedrich, S. Geibel, R. Kalmbach, I. Chizhov, K. Ataka, J. Heberle, M. Engelhard, E. Bamberg, Proteorhodopsin is a light-driven proton pump with variable vectoriality, J. Mol. Biol., 2002, 321, 821-838. 

  57. Science M H Stowell 276 812 1997 10.1126/science.276.5313.812 M. H. Stowell, T. M. McPhillips, D. C. Rees, S. M. Soltis, E. Abresch, G. Feher, Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer, Science, 1997, 276, 812-816. 

  58. Biochemistry R Hienerwadel 31 5799 1992 10.1021/bi00140a016 R. Hienerwadel, D. Thibodeau, F. Lenz, E. Nabedryk, J. Breton, W. Kreutz, W. Mantele, Time-resolved infrared spectroscopy of electron transfer in bacterial photosynthetic reaction centers: dynamics of binding and interaction upon QA and QB reduction, Biochemistry, 1992, 31, 5799-5808. 

  59. Biochemistry R Hienerwadel 34 2832 1995 10.1021/bi00009a013 R. Hienerwadel, S. Grzybek, C. Fogel, W. Kreutz, M. Y. Okamura, M. L. Paddock, J. Breton, E. Nabedryk, W. Mäntele, Protonation of Glu L212 following QB-formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy, Biochemistry, 1995, 34, 2832-2843. 

  60. Appl. Spectrosc. J R Burie 47 1401 1993 10.1366/0003702934067559 J. R. Burie, W. Leibl, E. Nabedryk, J. Breton, Step-Scan FT-IR Spectroscopy of Electron-Transfer in the Photosynthetic Bacterial Reaction-Center, Appl. Spectrosc., 1993, 47, 1401-1404. 

  61. Photosynth. Res. A Mezzetti 75 161 2003 10.1023/A:1022867317267 A. Mezzetti, D. Seo, W. Leibl, H. Sakurai, J. Breton, Time-resolved step-scan FTIR investigation on the primary donor of the reaction center from the green sulfur bacterium Chlorobium tepidum, Photosynth. Res., 2003, 75, 161-169. 

  62. Nat. Struct. Biol. A Remy 10 637 2003 10.1038/nsb954 A. Remy, K. Gerwert, Coupling of light-induced electron transfer to proton uptake in photosynthesis, Nat. Struct. Biol., 2003, 10, 637-644. 

  63. Biochemistry S Hermes 45 13741 2006 10.1021/bi060742q S. Hermes, J. M. Stachnik, D. Onidas, A. Remy, E. Hofmann, K. Gerwert, Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules, Biochemistry, 2006, 45, 13741-13749. 

  64. J. Biol. Chem. B C Hill 266 2219 1991 10.1016/S0021-9258(18)52231-6 B. C. Hill, The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen, J. Biol. Chem., 1991, 266, 2219-2226. 

  65. Biochemistry J W Thomas 32 10923 1993 10.1021/bi00091a048 J. W. Thomas, A. Puustinen, J. O. Alben, R. B. Gennis, M. Wikström, Substitution of asparagine for aspartate-135 in subunit I of the cytochrome bo ubiquinol oxidase of Escherichia coli eliminates proton-pumping activity, Biochemistry, 1993, 32, 10923-10928. 

  66. Biochemistry J A Garcia-Horsman 34 4428 1995 10.1021/bi00013a035 J. A. Garcia-Horsman, A. Puustinen, R. B. Gennis, M. Wikström, Proton transfer in cytochrome bo3 ubiquinol oxidase of Escherichia coli: second-site mutations in subunit I that restore proton pumping in the mutant Asp135→Asn, Biochemistry, 1995, 34, 4428-4433. 

  67. Science T Tsukihara 272 1136 1996 10.1126/science.272.5265.1136 T. Tsukihara, H. Aoyama, E. Yamashita, T. Tomizaki, H. Yamaguchi, K. Shinzawa-Itoh, R. Nakashima, R. Yaono, S. Yoshikawa, The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å, Science, 1996, 272, 1136-1144. 

  68. Nature S Iwata 376 660 1995 10.1038/376660a0 S. Iwata, C. Ostermeier, B. Ludwig, H. Michel, Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature, 1995, 376, 660-669. 

  69. J. Mol. Biol. M Svensson-Ek 321 329 2002 10.1016/S0022-2836(02)00619-8 M. Svensson-Ek, J. Abramson, G. Larsson, S. Tornroth, P. Brzezinski, S. Iwata, The X-ray Crystal Structures of Wild-type and EQ(I-286) Mutant Cytochrome c Oxidases from Rhodobacter sphaeroides, J. Mol. Biol., 2002, 321, 329-339. 

  70. Proc. Natl. Acad. Sci. U. S. A. E A Gorbikova 105 10733 2008 10.1073/pnas.0802512105 E. A. Gorbikova, I. Belevich, M. Wikstrom, M. I. Verkhovsky, The proton donor for O-O bond scission by cytochrome c oxidase, Proc. Natl. Acad. Sci. U. S. A., 2008, 105, 10733-10737. 

  71. Proc. Natl. Acad. Sci. U. S. A. R M Nyquist 100 8715 2003 10.1073/pnas.1530408100 R. M. Nyquist, D. Heitbrink, C. Bolwien, R. B. Gennis, J. Heberle, Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase, Proc. Natl. Acad. Sci. U. S. A., 2003, 100, 8715-8720. 

  72. J. Biol. Chem. F G Fiamingo 257 1639 1982 10.1016/S0021-9258(19)68085-3 F. G. Fiamingo, R. A. Altschuld, P. P. Moh, J. O. Alben, Dynamic interactions of CO with a3Fe and CuB in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures, J. Biol. Chem., 1982, 257, 1639-1650. 

  73. J. Biol. Chem. F G Fiamingo 261 12976 1986 10.1016/S0021-9258(18)69258-0 F. G. Fiamingo, R. A. Altschuld, J. O. Alben, Alpha and beta forms of cytochrome c oxidase observed in rat heart myocytes by low temperature Fourier transform infrared spectroscopy, J. Biol. Chem., 1986, 261, 12976-12987. 

  74. J. Am. Chem. Soc. R B Dyer 111 7657 1989 10.1021/ja00201a080 R. B. Dyer, O. Einarsdottir, P. M. Killough, J. J. Lopez-Garriga, W. H. Woodruff, Transient Binding of Photodissociated CO to CuB+ of Eukaryotic Cytochrome Oxidase at Ambient Temperature. Direct Evidence from Time-Resolved Infrared Spectroscopy, J. Am. Chem. Soc., 1989, 111, 7657-7659. 

  75. Biochemistry O Einarsdottir 32 12013 1993 10.1021/bi00096a011 O. Einarsdottir, R. B. Dyer, D. D. Lemon, P. M. Killough, S. M. Hubig, S. J. Atherton, J. J. Lopez-Garriga, G. Palmer, W. H. Woodruff, Photodissociation and recombination of carbonmonoxy cytochrome oxidase: dynamics from picoseconds to kiloseconds, Biochemistry, 1993, 32, 12013-12024. 

  76. Biophys. J. D Heitbrink 82 1 2002 10.1016/S0006-3495(02)75368-X D. Heitbrink, H. Sigurdson, C. Bolwien, P. Brzezinski, J. Heberle, Transient binding of CO to CuB in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: a time-resolved step-scan Fourier transform infrared investigation, Biophys. J., 2002, 82, 1-10. 

  77. J. Biol. Chem. K Koutsoupakis 277 32860 2002 10.1074/jbc.M204943200 K. Koutsoupakis, S. Stavrakis, E. Pinakoulaki, T. Soulimane, C. Varotsis, Observation of the equilibrium Cu-B-CO complex and functional implications of the transient heme a(3) propionates in cytochrome ba(3)-CO from Thermus thermophilus -Fourier transform infrared (FTIR) and time-resolved step-scan FTIR studies, J. Biol. Chem., 2002, 277, 32860-32866. 

  78. Biophys. J. C Koutsoupakis 86 2438 2004 10.1016/S0006-3495(04)74300-3 C. Koutsoupakis, T. Soulimane, C. Varotsis, Probing the Q-proton pathway of ba3-cytochrome c oxidase by time-resolved Fourier transform infrared spectroscopy, Biophys. J., 2004, 86, 2438-2444. 

  79. EMBO J. T Soulimane 19 1766 2000 10.1093/emboj/19.8.1766 T. Soulimane, G. Buse, G. P. Bourenkov, H. D. Bartunik, R. Huber, M. E. Than, Structure and mechanism of the aberrant ba(3)-cytochrome c oxidase from thermus thermophilus, EMBO J., 2000, 19, 1766-1776. 

  80. J. Am. Chem. Soc. C Koutsoupakis 125 14728 2003 10.1021/ja036107e C. Koutsoupakis, T. Soulimane, C. Varotsis, Ligand binding in a docking site of cytochrome c oxidase: A time-resolved step-scan Fourier transform infrared study, J. Am. Chem. Soc., 2003, 125, 14728-14732. 

  81. J. Am. Chem. Soc. S Stavrakis 124 3814 2002 10.1021/ja0169825 S. Stavrakis, K. Koutsoupakis, E. Pinakoulaki, A. Urbani, M. Saraste, C. Varotsis, Decay of the transient Cu(B)-CO complex is accompanied by formation of the heme Fe-CO complex of cytochrome cbb(3)-CO at ambient temperature: evidence from time-resolved Fourier transform infrared spectroscopy, J. Am. Chem. Soc., 2002, 124, 3814-3815. 

  82. Biochemistry M Oliveberg 30 7053 1991 10.1021/bi00243a003 M. Oliveberg, B. G. Malmström, Internal electron transfer in cytochrome c oxidase: evidence for a rapid equilibrium between cytochrome a and the bimetallic site, Biochemistry, 1991, 30, 7053-7057. 

  83. Biochemistry S Hallén 33 1467 1994 10.1021/bi00172a024 S. Hallén, P. Brzezinski, B. G. Malmström, Internal electron transfer in cytochrome c oxidase is coupled to the protonation of a group close to the bimetallic site, Biochemistry, 1994, 33, 1467-1472. 

  84. Biochemistry P Ädelroth 34 2844 1995 10.1021/bi00009a014 P. Ädelroth, P. Brzezinski, B. G. Malmström, Internal electron transfer in cytochrome c oxidase from Rhodobacter sphaeroides, Biochemistry, 1995, 34, 2844-2849. 

  85. Biochemistry B Rost 38 7565 1999 10.1021/bi990225q B. Rost, J. Behr, P. Hellwig, O. M. Richter, B. Ludwig, H. Michel, W. Mäntele, Time-Resolved FT-IR Studies on the CO Adduct of Paracoccus denitrificans Cytochrome c Oxidase: Comparison of the Fully Reduced and the Mixed Valence Form, Biochemistry, 1999, 38, 7565-7571. 

  86. Biochemistry E A Gorbikova 46 13141 2007 10.1021/bi701614w E. A. Gorbikova, N. P. Belevich, M. Wikstrom, M. I. Verkhovsky, Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans, Biochemistry, 2007, 46, 13141-13148. 

  87. Acc. Chem. Res. R B Dyer 31 709 1998 10.1021/ar970343a R. B. Dyer, F. Gai, W. H. Woodruff, Infrared studies of fast events in protein folding, Acc. Chem. Res., 1998, 31, 709-716. 

  88. J. Am. Chem. Soc. C Y Huang 123 12111 2001 10.1021/ja016631q C. Y. Huang, Z. Getahun, T. Wang, W. F. DeGrado, F. Gai, Time-resolved infrared study of the helix-coil transition using C-13-labeled helical peptides, J. Am. Chem. Soc., 2001, 123, 12111-12112. 

  89. Proc. Natl. Acad. Sci. U. S. A. M C Asplund 97 8219 2000 10.1073/pnas.140227997 M. C. Asplund, M. T. Zanni, R. M. Hochstrasser, Two-dimensional infrared spectroscopy of peptides by phase-controlled femtosecond vibrational photon echoes, Proc. Natl. Acad. Sci. U. S. A., 2000, 97, 8219-8224. 

  90. Science P Kukura 310 1006 2005 10.1126/science.1118379 P. Kukura, D. W. McCamant, S. Yoon, D. B. Wandschneider, R. A. Mathies, Structural observation of the primary isomerization in vision with femtosecond-stimulated Raman, Science, 2005, 310, 1006-1009. 

섹션별 컨텐츠 바로가기

AI-Helper ※ AI-Helper는 오픈소스 모델을 사용합니다.

AI-Helper 아이콘
AI-Helper
안녕하세요, AI-Helper입니다. 좌측 "선택된 텍스트"에서 텍스트를 선택하여 요약, 번역, 용어설명을 실행하세요.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.

선택된 텍스트

맨위로