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Effect of neutral and acidic phospholipids on mitochondrial ATP synthase secondary structure
Author(s) -
Sala Federica Dabbeni,
Loregian Arianna,
Lippe Giovanna,
Bertoli Enrico,
Tanfani Fabio
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80859-s
Subject(s) - atp synthase , phosphatidylcholine , phospholipid , chemistry , enzyme , atpase , biochemistry , mitochondrion , biology , membrane
The secondary structure of delipidated and egg phosphatidylcholine or asolectin reconstituted mitochondrial ATP synthase complex from beef heart was investigated by Fourier transform infrared spectroscopy. Upon reconstitution, the infrared spectra of ATP synthase revealed an increase in turns and a concomitant decrease in β‐sheet content which occurred to a larger extent in the presence of asolectin rather than in the presence of egg phosphatidylcholine. These data correlate with kinetic data showing a higher ATPase activity of the asolectin reconstituted enzyme protein than the egg phosphatidylcholine reconstituted or delipidated enzyme complexes.