ABSTRACT
Raman spectroscopy has emerged as an extremely powerful and informative technique for probing the structure and chemistry of biological molecules. Some specific points for the study of quinoproteins are briefly summarized. The authors have found that high quality resonance Raman spectra can be obtained on quinoproteins and certain derivatives when the sample absorbance is approximately in the range of 3-7 for a 1-cm pathlength. Additional experiments have shown that a wide variety of quinones and other carbonyl compounds may be distinguished via resonance Raman spectroscopy of their hydrazine derivatives, especially if two derivatives are examined. In many respects resonance Raman spectroscopy has already proven to be a valuable technique in the study of quinones and quinoproteins. This growth will come from an increase in the number of quinoproteins investigated and from the desire to probe the active-site structure and reactivity of previously characterized proteins in greater detail and with greater sophistication.
