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Resonance Raman Spectroscopic Characterization of the Oxidation of the Horseradish Peroxidase Active Site

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Charge and Field Effects in Biosystems—2

Abstract

Enzymes containing heme prosthetic groups (heme enzymes) are an extensive class of biological catalysts. These enzymes possess differing reactivities and specificities, even though they contain a very similar active site heme group, which is in many cases an unmodified iron-bound protoporphyrin IX. Some heme enzymes of current interest include cytochrome P-450, cytochrome oxidase, tryptophan pyrollase, prostaglandin synthase, secondary amine mono-oxygenase, ligninase and the various peroxidases and catalases [1–3]. The ability of the heme enzymes to mediate reactions involving oxygen is of importance to industrial applications and health related areas [4].

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Authors and Affiliations

  1. Dept. of Chemistry, Virginia Commonwealth University, Richmond, Virginia, 23284-2006, USA

    James Terner, Andrew J. Sitter & John R. Shifflett

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  1. James Terner
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  1. Virginia Commonwealth University, Richmond, Virginia, USA

    M. J. Allen , S. F. Cleary  & F. M. Hawkridge ,  & 

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© 1989 Plenum Press, New York

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Terner, J., Sitter, A.J., Shifflett, J.R. (1989). Resonance Raman Spectroscopic Characterization of the Oxidation of the Horseradish Peroxidase Active Site. In: Allen, M.J., Cleary, S.F., Hawkridge, F.M. (eds) Charge and Field Effects in Biosystems—2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0557-6_4

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  • DOI: https://doi.org/10.1007/978-1-4613-0557-6_4

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