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Generation of energy during CO/sub 2/ fixation in acetogenic bacteria

Thesis/Dissertation ·
OSTI ID:6281078

The F/sub 1/-ATPase from Clostridium thermoaceticum and the F/sub 1/-F/sub 0/-ATPase from C. thermoautotrophicum have been purified and characterized. The F/sub 1/ is a 370,000 M/sub r/ complex with four types of subunit with M/sub r/ values of 60,000, 55,000, 37,000, and 17,000, in a molar ratio of 3:3:1:1. Purified F/sub 1/ would rebind to stripped membranes to reconstitute DCCD-sensitive ATPase activity. Membrane vesicles and the F/sub 1/ were examined by electron microscopy. F/sub 1/-ATPase particles projecting from the vesicles have a diameter of 10 to 12 nm. The alpha and beta subunits are most likely arranged in an alternating sequence around a central mass consisting of the gamma and delta subunits. The F/sub 1/F/sub 0/-ATPase from C. thermoautotrophicum has an apparent minimum subunit composition of six non-identical polypeptides, four of which comprise F/sub 1/ and two, with M/sub r/ values of 21,000 and 12,300, of which comprise F/sub 0/. ATP hydrolysis catalyzed by the purified enzyme was inhibited approximately 50% by DCCD. Inhibition of F/sub 1/F/sub 0/ with (/sup 14/C)DCCD resulted in the labeling of the 12,300-dalton subunit of F/sub 0/. The complex has been reconstituted with phospholipids into proteoliposomes which demonstrate ATP-P/sub i/ exchange activity, FCCP-stimulated ATPase activity, and ATP-dependent proton pumping.

Research Organization:
Georgia Univ., Athens (USA)
OSTI ID:
6281078
Country of Publication:
United States
Language:
English