Abstract
A simple and versatile system for resonance Raman (RR) spectroscopic analysis of enzymesubstrate complexes at liquid helium temperatures is described. The system allows us to record high-quality RR spectra for dithioacyl papain intermediates (MeO-Phe-Gly- and MeO-Gly-Gly-Phe-Gly-C (S)S-papain) in ice matrices at 5 K. Based on established structure-spectra correlations, it is concluded that the active-site conformation of the intermediates about the φ′, ψ′ glycinic linkages and cysteine-25 side chain is B-G+-PH both in ice matrices at 5 K and in solution at room temperature.
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