TY - JOUR
T1 - Nanosecond time-resolved fluorescence investigations of temperature-induced conformational changes in cytochrome oxidase in phosphatidylcholine vesicles and solubilized systems
AU - Kawato, Suguru
AU - Yoshida, Satoshi
AU - Orii, Yutaka
AU - Ikegami, Akira
AU - Kinosita, Kazuhiko
PY - 1981
Y1 - 1981
N2 - Intrinsic and lipid phase transition-induced conformational changes in cytochrome oxidase in phosphatidylcholine vesicle and solubilized systems were examined by the fluorescence lifetime of N-(1-anilinonaphthyl-4)-maleimide conjugated with the enzyme. The time-dependent fluorescence intensity of N-(1-anilinonaphthyl-4)-maleimide attached to cytochrome oxidase was described as a triple exponential decay. Both the intrinsic and lipid phase transition-induced conformational changes were detectable in plots of the average lifetime against temperature. In most cases a peak occurred at the temperature of the conformational change. The time-dependent emission anisotropy showed that N-(1-anilinonaphthyl-4)-maleimide embedded in cytochrome oxidase in phosphatidylcholine vesicles underwent a rapid restricted wobbling within a cone. The half-angle of the cone was around 30° for cytochrome oxidase in dimyristoyl phosphatidylcholine vesicles.
AB - Intrinsic and lipid phase transition-induced conformational changes in cytochrome oxidase in phosphatidylcholine vesicle and solubilized systems were examined by the fluorescence lifetime of N-(1-anilinonaphthyl-4)-maleimide conjugated with the enzyme. The time-dependent fluorescence intensity of N-(1-anilinonaphthyl-4)-maleimide attached to cytochrome oxidase was described as a triple exponential decay. Both the intrinsic and lipid phase transition-induced conformational changes were detectable in plots of the average lifetime against temperature. In most cases a peak occurred at the temperature of the conformational change. The time-dependent emission anisotropy showed that N-(1-anilinonaphthyl-4)-maleimide embedded in cytochrome oxidase in phosphatidylcholine vesicles underwent a rapid restricted wobbling within a cone. The half-angle of the cone was around 30° for cytochrome oxidase in dimyristoyl phosphatidylcholine vesicles.
KW - (Nanosecond spectroscopy)
KW - Conformational change
KW - Cytochrome oxidase
KW - Fluorescence anisotropy
KW - Phase transition
KW - Phosphatidylcholine vesicle
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U2 - 10.1016/0005-2728(81)90129-8
DO - 10.1016/0005-2728(81)90129-8
M3 - Article
C2 - 6258646
AN - SCOPUS:0019879477
SN - 0005-2728
VL - 634
SP - 85
EP - 92
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
IS - C
ER -