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Study of the Lipid‐Protein Interaction of F ATPases
Author(s) -
YANG F. Y.
Publication year - 1992
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1992.tb43812.x
Subject(s) - atpase , chemistry , biophysics , conformational change , lipid bilayer , biochemistry , chloroplast , mitochondrion , f atpase , membrane , microbiology and biotechnology , enzyme , biology , thylakoid , gene
Mg2+ may play a role in altering the lipid fluidity of the bilayers which would induce a change in conformation of the F0 portion of the H(+)-ATPase complex. This change could be transmitted to the soluble F1 portion, the conformation of which is in turn altered, resulting in higher enzymic activity. In addition to mitochondrial H(+)-ATPase, similar Mg2+ effects on the reconstitution of chloroplast H(+)-ATPase and other intrinsic membrane proteins have also been observed in our laboratory.