Summary
Horseradish peroxidase was homogeneously solubilized in benzene by the covalent modification of lysine residues on the protein surface with polyethylene glycol. The addition of a stoichiometric quantity of hydrogen peroxide to polyethylene-glycolated horseradish peroxidase in benzene gave the compound I chromophore. In the presence of a large excess of guaiacol, compound I was reduced first to compound II and then to the ferric enzyme. Thus, catalytic intermediates in benzene were the ferryl species as established in aqueous buffer. The slower reduction of compound I with guaiacol in benzene than in buffer suggested that the accessibility of the active site for the substrates decreases in benzene.
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© 1998 Springer-Verlag Tokyo
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Ozaki, SI., Inada, Y., Watanabe, Y. (1998). Catalytic Intermediates of Polyethylene-Glycolated Horseradish Peroxidase in Benzene. In: Ishimura, Y., Shimada, H., Suematsu, M. (eds) Oxygen Homeostasis and Its Dynamics. Keio University Symposia for Life Science and Medicine, vol 1. Springer, Tokyo. https://doi.org/10.1007/978-4-431-68476-3_45
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DOI: https://doi.org/10.1007/978-4-431-68476-3_45
Publisher Name: Springer, Tokyo
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