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J. Biol. Chem., Vol. 264, Issue 11, 6183-6187, Apr, 1989
L Calabrese, M Carbonaro and G Musci
The reactivity with dioxygen of a mammalian (sheep) ceruloplasmin,
anaerobically reduced with ascorbate, was found to depend on the state of
the Type 2 and Type 3 copper centers, as monitored by EPR and optical
spectroscopy. A complete reoxidation by air after anaerobic reduction with
ascorbate was observed with samples (A) purified by the single-step
procedure described for chicken ceruloplasmin (Calabrese, L., Carbonaro,
M., and Musci, G. (1988) J. Biol. Chem. 263, 6480-6483), while samples
prepared by traditional multistep procedure (B) or subjected to
freeze-thawing (C) displayed partial and very slow reoxidation, reflecting
the functional nonequivalence of blue coppers which is considered a typical
property of mammalian ceruloplasmin. The rate of reduction of the 330 nm
chromophore was found to increase as a function of the extent and rate of
reoxidation of different samples, while the 610 nm band displayed an
opposite trend. Samples B and C showed a Type 2 copper signal in the EPR
spectrum, while sample A showed practically no Type 2 copper in the
oxidized protein, and a transient Type 2-like signal during reduction. The
presence of a trinuclear Type 2-Type 3 cluster can therefore be proposed
for all ceruloplasmins, and the integrity of the copper-copper coupling is
essential for efficient oxidase behavior.
Presence of coupled trinuclear copper cluster in mammalian ceruloplasmin is essential for efficient electron transfer to oxygen
Department of Biochemical Sciences, Universita La Sapienza, Roma, Italy.
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