FOURIER-TRANSFORM RAMAN-SPECTROSCOPY OF PHOTOACTIVE PROTEINS WITH NEAR-INFRARED EXCITATION

被引：28

作者：

JOHNSON, CK ^{[1
]}

RUBINOVITZ, R ^{[1
]}

机构：

[1] BRUKER INSTRUMENTS INC,BILLERICA,MA 01821

来源：

APPLIED SPECTROSCOPY | 1990年 / 44卷 / 07期

关键词：

D O I：

10.1366/0003702904086434

中图分类号：

TH7 [仪器、仪表];

学科分类号：

0804 ; 080401 ; 081102 ;

摘要：

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.

引用

页码：1103 / 1106

页数：4

共 23 条

[1] NEAR-INFRARED-EXCITATION RESONANCE RAMAN-SPECTRA OF BACTERIAL PHOTOSYNTHETIC REACTION CENTERS - IMPLICATIONS FOR PATH-SPECIFIC ELECTRON-TRANSFER [J].