文章基本信息

标题：Resonance coherent anti-Stokes Raman scattering spectra of fluorescent biological chromophores: Vibrational evidence for hydrogen bonding of flavin to glucose oxidase and for rapid solvent exchange
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作者：Prabir K. Dutta ; James R. Nestor ; Thomas G. Spiro 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1977
卷号：74
期号：10
页码：4146-4149
DOI：10.1073/pnas.74.10.4146
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Coherent anti-Stokes Raman scattering (CARS) spectra are reported for flavin adenine dinucleotide (FAD) and glucose oxidase ({beta}-D-glucose:oxygen 1-oxidoreductase; EC 1.1.3.4 ), in resonance with the 450 nm flavin absorption band. Several isoalloxazine ring modes were observed (1635, 1584, 1507, 1416, and 1359 cm-1). A 12 cm-1 increase in one component of the 1359 cm-1 band upon binding to glucose oxidase was attributed to hydrogen bonding of the N3 proton to a protein acceptor. This interpretation is consistent with deuteration results. Smaller decreases (5-7 cm-1) on binding were observed for the 1635 and 1416 cm-1 modes (and also a 1297 cm-1 mode of deuterated FAD) and were attributed to environmental effects. Deuteration of bound FAD was observed within 5 min of mixing glucose oxidase with D2O, demonstrating ready access to solvent. Lorentzian CARS peaks were observed with {omega}as at the peak of the 450 nm absorption band, a condition which corresponds to maximum resonance enhancement if the peak corresponds to the envelope of 0-1 vibronic transitions. If {omega}1 was tuned to the peak, then dispersion lineshapes were observed, reflecting a loss of Raman enhancement relative to the electronic background.
关键词：flavoprotein ; nonlinear optics ; coherent anti-Stokes Raman scattering lineshapes