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[18] Resonance Raman spectroscopy of metalloproteins

1995; Academic Press; Linguagem: Inglês

10.1016/0076-6879(95)46020-9

1557-7988

Thomas G. Spiro, Roman S. Czernuszewicz,

Protein Interaction Studies and Fluorescence Analysis

This chapter discusses how metal ion environments in metalloproteins and metalloenzymes can be studied by resonance Raman (RR) spectroscopy. The chapter describes experimental techniques and methods of analysis and interpretation by using selected examples. The ability of RR spectroscopy to identify the presence or absence of particular structural units, and the ligation modes of the amino acids, has made the technique especially powerful in studies of protein structure and function. The central advantage of RR spectroscopy is that, when the wavelength of the exciting laser line is adjusted to coincide with that of an allowed electronic transition in a molecule, the intensities of certain Raman bands are enhanced relative to the off-resonance values. The technique is therefore more sensitive than normal (off-resonance) Raman spectroscopy. Resonance Raman scattering occurs when a material is irradiated with monochromatic light corresponding to an allowed absorption band region. The effect is studied by examining the intensity of scattered photons as a function of the proximity of the excitation wavelength to electronic absorption bands of the molecule.