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Surface-enhanced resonance Raman scattering (SERRS) studies of cytochrome P-450j,, myoglobin, and cytochrome ç have demonstrated that the native structure of hemecontaining proteins can be retained at SERRS-active substrates. However, certain adsorption parameters must be maintained in order to preserve the native state of the adsorbed species. Our work shows that the optimal adsorption conditions depend upon the nature of the protein Spectra relevant to unperturbed cyt P-450̂ were obtained only when SERRS-active electrodes were subjected to liquid nitrogen temperatures. Under these same conditions, the band frequencies of myoglobin indicated that the heme environment was indeed perturbed. The native state of the protein was retained only when myoglobin was adsorbed onto citrate-reduced sols or onto an electrode roughened in the presence of citrate. In contrast, cyt c is stable at different SERRS-active substrates, including electrochemically-roughened silver electrodes, silver-island films and citrate-reduced silver sols. In order to retain the native integrity of cyt s, the adsorption conditions at the SERRS-active substrates must also be established. The results support the enormous potential of SERRS as a

Preparation of surface-enhanced resonance Raman scattering-active substrates: applications to heme-containing proteins