LOW-TEMPERATURE OPTICAL SPECTROSCOPY - METALLOPROTEIN STRUCTURE AND DYNAMICS

This chapter recounts outlines the history of the topic and presents an appropriate context to the value and proper status of low-temperature studies in revealing secrets of the structure-function relationships of metalloproteins. The values of low-temperature optical studies are many. Some of the obvious advantages these investigations often have over those at ambient temperatures are that they allow (1) the trapping or isolation of reactive species, (2) increased resolution of spectral bands, (3) probing of conformational dynamics and broadening mechanisms based on temperature-dependent changes in optical bands, and (4) examination of electron-nuclear coupling strengths by comparison of optical and resonance Raman theory and experiment. This chapter presents examples of the way both historical and current experiments capitalize on these four points and suggests some suitable areas for future research. Developments in the application of the technique have been evidenced by the expanding utilization of low-temperature optical spectroscopy to probe metailoprotein structure and dynamics. Specifically, analysis of low-temperature optical data to understand structure in heme proteins has seen an acceleration of interest. The use of the “optical method” in biophysics has been reviewed, and this chapter discusses these new applications and attempts to trace some of their historical origins. © 1993, Academic Press, Inc.