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Lecture 13

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Department
Biology (Sci)
Course
BIOL 201
Professor
Greg Brown
Semester
Winter

Description
Lecture 13 ATP Synthase Through Chemiosmotic Oxidative Phosphorylation ATP synthase has 2 parts F1 and F0 F1 has 5 further subunits 3 alphas 3 betas gamma delta epsilon alpha and beta exists in a triplet of dimers F0 extends into the intermembrane space F0 has 3 subunits 1 a subunit 2 b subunits and 1 c subunit Gamma epsilon and c are capable of rotating Ab delta alphabeta dimers are stationary As the rotating subunits rotate gamma subunit brushes against the alphabeta dimers The rotation itself is caused by the discharge of the proton gradient the rotation causes conformational changes in the gamma subunit The a subunit has 2 half channel which is a channel for half of the distance After entering a half channel the proton can associate with the c subunitThe c subunit moves into the membrane itself away from the a subunit The number of c subunits could range from 10 to 14 in organisms Aspartic acid residues on the outside of the subunit c The two half channel of subunit a one from intermembrane into the membrane and the other from the membrane to the matrix Rotation caused by the charge cancellation of protons by the aspartic acid Rotates counterclockwise when flowing from up to down The gamma subunit itself is asymmetrical 3 faces to the gamma subunit Depending on which face is attached to which beta subunit the beta conformation will change The 3 conformations areO L and T O ha
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