Interaction between delta and epsilon subunits of F1-ATPase from pig heart mitochondria. Circular dichroism and intrinsic fluorescence of purified and reconstituted delta epsilon complex.
A delta epsilon complex has been purified as a molecular entity from pig heart mitochondrial F1-ATPase. This delta epsilon complex has also been reconstituted from purified delta and epsilon subunits. Both isolated and reconstituted delta epsilon complexes have delta 1 epsilon 1 stoichiometry and are indistinguishable by their chromatographic behavior, their circular dichroism spectra (CD spectra), and their intrinsic fluorescence features. The content of secondary structures deduced from CD spectra of the delta epsilon complex appears to be the sum of the respective contributions of purified delta and epsilon subunits. All intrinsic fluorescence studies carried out on isolated epsilon subunit and delta epsilon complex show that the single tryptophan residue located on epsilon is involved in the interaction between delta and epsilon subunits. Results obtained with F1-ATPase are in favor of the same delta epsilon interaction in the entire enzyme.
Penin
F
F
Laboratoire de Biologie et Technologie des Membranes du CNRS, Université Claude Bernard de Lyon, Villeurbanne, France.
Deléage
G
G
Gagliardi
D
D
Roux
B
B
Gautheron
D C
DC
D000818:Animals; D002850:Chromatography, Gel; D002942:Circular Dichroism; D008929:Mitochondria, Heart / Q000201:enzymology; D008970:Molecular Weight; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000302:isolation & purification; D013050:Spectrometry, Fluorescence; D013552:Swine; D014364:Tryptophan / Q000737:chemistry
D014364:Tryptophan; D006180:Proton-Translocating ATPases