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The Second Stalk of the FoF1‐ATP synthase
Author(s) -
Wise John G,
Hornung Tassilo,
Dunn Stanley D.,
Hustedt Eric J.,
Vogel Pia D.
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a893-b
Subject(s) - atp synthase , dimer , protein quaternary structure , atp synthase gamma subunit , cysteine , chemistry , protein subunit , molecular dynamics , biochemistry , biophysics , crystallography , enzyme , atpase , computational chemistry , biology , gene , atp hydrolysis , organic chemistry
The detailed structure and the protein‐protein interactions of the stator subunits of the F1Fo‐ATP synthase remain one of the important questions in the ATP synthase field since these interactions are directly related to the mechanics of energy conservation and storage of rotational energy during catalytic turnover. Understanding the structures and interactions is therefore crucial to the understanding of the overall catalytic mechanism of the synthase and especially that of energy transduction within the protein. We have used ESR and site‐specific spin‐labeling to gain further insight into the quaternary structure of the dimer formed by the subunits b of the Fo‐sub‐complex of the FoF1‐ATPsynthase. We introduced at total of 37 individual cysteine mutations into a water‐soluble mutant of the b‐dimer and have specifically spin‐labeled them with different cysteine‐specific spin‐labels. The distances between the spin‐labels within the b‐dimer were determined using low‐temperature ESR. We are using the distance constraints we obtained from ESR spectroscopy and molecular modeling and molecular dynamics techniques to determine the quaternary structure interactions of the dimer of b‐subunits. The data obtained by ESR will be compared to di‐sulfide cross linking pattern of the proteins.