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A study of the mitochondrial F1-ATPase tryptophan phosphorescence at 273 K.

Abstract：

:The bovine heart mitochondrial F1-ATPase complex exhibits an intrinsic tryptophan phosphorescence that can be used to monitor structural changes of the epsilon-subunit. The phosphorescence decay rate of F1 containing the tightly bound nucleotides increases upon addition of adenine nucleoside triphosphate in the presence of magnesium. The average phosphorescence lifetime of this enzyme preparation decreases from 10.2 to 7.8 ms upon Mg-ATP addition. Since increasing phosphorescence decay rate is related to increasing flexibility of proteins, Mg-ATP added to the F1-ATPase complex can enhance the flexibility of the protein structure surrounding the chromophore. Experiments carried out on F1 prepared with the three noncatalytic sites filled and the three catalytic sites vacant show a significant increase of the phosphorescence lifetime from 6.4 ms to 7.6 ms upon Mg-ATP addition. These results suggest that the mitochondrial F1-ATPase epsilon-subunit conformation senses differently the nucleoside triphosphate binding to catalytic or noncatalytic sites.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Baracca A,Barogi S,Gabellieri E,Lenaz G,Solaini G

doi

10.1006/bbrc.1995.1197

subject

Has Abstract

pub_date

1995-02-06 00:00:00

pages

369-74

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(85)71197-7

journal_volume

207

pub_type

杂志文章

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