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1. The major EPR signals from native and cytochrome c-reduced beef heart cytochrome c oxidase (EC 1.9.3.1) are characterized with respect to resonance parameters, number of components and total integrated intensity. A mistake in all earlier integrations and simulations of very anisotropic EPR signals is pointed out. 2. The so-called Cu2+ signal is found to contain at least three components, one "inactive" form and two nearly similar active forms. One of the latter forms, corresponding to about 20% of the total EPR detectable Cu, has not been observed earlier and can only be resolved in 35 GHz spectra. It is not reduced by cytochrome c and is thought to reflect some kind of inhomogeneity in the enzyme preparation. The 35 GHz spectrum of the cytochrome c reducible component shows a rhombic splitting and can be well simulated with g-values 2.18, 2.03 and 1.99. The origin of such a unique type of Cu2+ spectrum is discussed. 3. The low-spin heme signal in the oxidized enzyme (g = 3.03, 2.21, 1.45) is found to correspond closely to one heme and shows no signs of interaction with other paramagnetic centres. 4. The high-spin heme signals appearing in partly reduced oxidase are found to consist of at least three species, one axial and two rhombic types. An integration procedure is described that allows the determination of the total integral intensity of high-spin heme EPR signals only by considering the g = 6 part of the signals. In a titration with ascorbate and cytochrome c the maximum intensity of the g = 6 species corresponds to 23% of the enzyme concentration.
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
January 2001,
Journal of inorganic biochemistry,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
December 1974,
Biochimica et biophysica acta,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
April 2007,
The journal of physical chemistry. B,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
June 1984,
Biochimica et biophysica acta,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
January 1979,
FEBS letters,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
September 1992,
The Journal of biological chemistry,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
January 1980,
Biochemical and biophysical research communications,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
February 1976,
Biochimica et biophysica acta,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
February 1982,
The Biochemical journal,
R Aasa, and
P J Albracht, and
K E Falk, and
B Lanne, and
T Vänngard
February 1977,
FEBS letters,
