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

Radu I, Schleeger M, Bolwien C, Heberle J (2009)
PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES 8(11): 1517-1528.

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Abstract
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 NMR and X-ray crystallography are challenged by the size and protein hydrophobicity, as well as by their limited time-resolution. Here, we summarize the principles and experimental realizations of time-resolved FT-IR spectroscopy developed in our group and compare with aspects emerging from other laboratories. Examples of applications to retinal proteins and energy transduction complexes are reviewed, which emphasize the impact of time-resolved FT-IR spectroscopy on the understanding of protein reactions on the level of single bonds.
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Radu I, Schleeger M, Bolwien C, Heberle J. Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins. PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES. 2009;8(11):1517-1528.
Radu, I., Schleeger, M., Bolwien, C., & Heberle, J. (2009). Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins. PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES, 8(11), 1517-1528.
Radu, I., Schleeger, M., Bolwien, C., and Heberle, J. (2009). Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins. PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES 8, 1517-1528.
Radu, I., et al., 2009. Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins. PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES, 8(11), p 1517-1528.
I. Radu, et al., “Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins”, PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES, vol. 8, 2009, pp. 1517-1528.
Radu, I., Schleeger, M., Bolwien, C., Heberle, J.: Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins. PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES. 8, 1517-1528 (2009).
Radu, Ionela, Schleeger, Michael, Bolwien, Carsten, and Heberle, Joachim. “Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins”. PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES 8.11 (2009): 1517-1528.
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89 References

Data provided by Europe PubMed Central.

Nano- and microsecond time-resolved FTIR spectroscopy of the halorhodopsin photocycle.
Dioumaev AK, Braiman MS., Photochem. Photobiol. 66(6), 1997
PMID: 9421962
The proton donor for O-O bond scission by cytochrome c oxidase.
Gorbikova EA, Belevich I, Wikstrom M, Verkhovsky MI., Proc. Natl. Acad. Sci. U.S.A. 105(31), 2008
PMID: 18664577
Bacteriorhodopsin: a light-driven proton pump in Halobacterium Halobium.
Lozier RH, Bogomolni RA, Stoeckenius W., Biophys. J. 15(9), 1975
PMID: 1182271
Spectrally silent transitions in the bacteriorhodopsin photocycle.
Chizhov I, Chernavskii DS, Engelhard M, Mueller KH, Zubov BV, Hess B., Biophys. J. 71(5), 1996
PMID: 8913574
Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle.
Sasaki J, Yuzawa T, Kandori H, Maeda A, Hamaguchi H., Biophys. J. 68(5), 1995
PMID: 7612850
Halide dependence of the halorhodopsin photocycle as measured by time-resolved infrared spectra.
Hutson MS, Shilov SV, Krebs R, Braiman MS., Biophys. J. 80(3), 2001
PMID: 11222305

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