MECHANISM OF ENANTIOSELECTIVE OXYGENATION OF SULFIDES CATALYZED BY CHLOROPEROXIDASE AND HORSERADISH-PEROXIDASE - SPECTRAL STUDIES AND CHARACTERIZATION OF ENZYME SUBSTRATE COMPLEXES
Articolo
Data di Pubblicazione:
1992
Citazione:
MECHANISM OF ENANTIOSELECTIVE OXYGENATION OF SULFIDES CATALYZED BY
CHLOROPEROXIDASE AND HORSERADISH-PEROXIDASE - SPECTRAL STUDIES AND
CHARACTERIZATION OF ENZYME SUBSTRATE COMPLEXES / L. CASELLA, M. GULLOTTI, R. GHEZZI, S. POLI, T. BERINGHELLI, S. COLONNA, G. CARREA. - In: BIOCHEMISTRY. - ISSN 0006-2960. - 31:39(1992), pp. 9451-9459.
Abstract:
The binding of a series of alkyl aryl sulfides to chloroperoxidase (CPO)
and horseradish peroxidase (HRP) has been investigated by optical
difference spectroscopy, circular dichroism, paramagnetic NMR
spectroscopy, and NMR relaxation measurements. The data are consistent
with binding of the sulfides in the distal side of the heme pocket with
CPO and near the heme edge with HRP. A linear correlation between the
binding constants of para-substituted sulfides to CPO and the Taft
sigma(I) parameter suggests that these substrates act as donors in
donor-acceptor complexes involving some residue of the protein chain.
Spectral studies during turnover show that high enantioselectivity in
the CPO-catalyzed oxidation of sulfides results from a reaction pathway
that does not involve the accumulation of compound II enzyme
intermediate.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
L. CASELLA, M. GULLOTTI, R. GHEZZI, S. POLI, T. BERINGHELLI, S. COLONNA, G. CARREA
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