Abstract

The Fourier transform (FT) Raman spectroscopic treatment of the photoactive proteins bacteriorhodopsin and the photosynthetic reaction center is reported, with excitation at 1.06 μm. Excitation at this wavelength circumvents the limitations on resonance Raman spectroscopy of these proteins imposed by their photolability and by the fluorescence of free pigments or impurities. The spectra are dominated by nonresonant Raman scattering by the protein-bound pigments retinal (in bacteriorhodopsin) and bacteriopheophytin, bacteriochlorophyll, and carotenoids (in reaction centers). The relative intensities of retinylidene modes in the spectrum for nonresonant FT Raman spectroscopy of bacteriorhodopsin are nearly identical to those observed in the resonance Raman spectrum of bacteriorhodopsin.

Measurement of two-photon excitation spectra of fluorescent proteins with nonlinear Fourier-transform spectroscopy

Hiroshi Hashimoto, Keisuke Isobe, Akira Suda, Fumihiko Kannari, Hiroyuki Kawano, Hideaki Mizuno, Atsushi Miyawaki, and Katsumi Midorikawa
Appl. Opt. 49(17) 3323-3329 (2010)

Measurement of two-photon excitation spectrum used to photoconvert a fluorescent protein (Kaede) by nonlinear Fourier-transform spectroscopy

Keisuke Isobe, Hiroshi Hashimoto, Akira Suda, Fumihiko Kannari, Hiroyuki Kawano, Hideaki Mizuno, Atsushi Miyawaki, and Katsumi Midorikawa
Biomed. Opt. Express 1(2) 687-693 (2010)

Polarized pump–probe spectroscopy of electronic excitation transport in photosynthetic antennas

Walter S. Struve
J. Opt. Soc. Am. B 7(8) 1586-1594 (1990)

Raman spectroscopy of gases with a Fourier transform spectrometer: the spectrum of D₂

Donald E. Jennings, A. Weber, and J. W. Brault
Appl. Opt. 25(2) 284-290 (1986)

New trends in the application of Fourier transform infrared spectroscopy to analytical chemistry

Tomas Hirschfeld
Appl. Opt. 17(9) 1400-1412 (1978)