Abstract
Microperoxidase-11, MP-11, heme-undecapeptide, prepared by pepsin digestion of cytochrome c, retains the proximal His ligand and two thioether bonds between iron-protoporphyrin IX and two Cys residues. The peroxidase activities of MPs have been demonstrated in the oxidation of so-called peroxidase’s substrates, phenolic compounds, in the presence of H2O2. MPs are unique and simple hemoprotein which are not restricted by consideration of the apoprotein structure. In this study, cytochrome P-450-like reactivities of MP-11, sulfide oxidation, N-dealkylation, and olefin epoxidation, were investigated1,2).
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References
T. Mashino, S. Nakamura, and M. Hirobe, Tetrahedron Lett., 31 ,3163 (1990).
S. Nakamura, T. Mashino, and M. Hirobe, Tetrahedron Lett ,33, 5409 (1992).
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© 1993 Springer Science+Business Media New York
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Nakamura, S., Mashino, T., Hirobe, M. (1993). Cytochrome P-450 Like Substrate Oxidation Catalyzed by Heme-Undecapeptide, Microperoxidase-11. In: Barton, D.H.R., Martell, A.E., Sawyer, D.T. (eds) The Activation of Dioxygen and Homogeneous Catalytic Oxidation. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3000-8_63
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DOI: https://doi.org/10.1007/978-1-4615-3000-8_63
Publisher Name: Springer, Boston, MA
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