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Volume 271, Number 46, Issue of November 15, 1996 pp. 28805-28811
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Resonance Raman Spectra of Native and Mesoheme-reconstituted Horseradish Peroxidase and Their Catalytic Intermediates

(Received for publication, November 9, 1995, and in revised form, August 12, 1996)

From the Chemistry Department, Marquette University, Milwaukee, Wisconsin 53201-1881

Resonance Raman studies of native and mesoheme-reconstituted horseradish peroxidase and their catalytic intermediates, known as Compounds I and II, have been conducted using both near UV (~350 nm) and visible (406.7 nm) excitation. Careful power studies indicate that the authentic Compound I spectra are obtainable using near UV excitation, but that use of visible excitation results in contamination of the Compound I spectrum with the spectrum of a Compound II-like photoproduct. Using H₂¹⁸O₂, the (Fe=O) stretching modes for both systems are unambiguously identified, for the first time, at ~790 cm¹. The authentic Compound I spectra are indicative of an ²A_1u-like ground state for both the native and the mesoheme-reconstituted proteins. Finally, the possible biological implications of such information are briefly discussed.

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