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Journal of Bacteriology, September 2003, p. 5527-5535, Vol. 185, No. 18
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.18.5527-5535.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Clostridium pasteurianum F₁F_o ATP Synthase: Operon, Composition, and Some Properties

Amaresh Das^1,2* and Lars G. Ljungdahl^1,2

Center for Biological Resource Recovery,¹ Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602²

Received 25 April 2003/ Accepted 23 June 2003

The atp operon encoding F₁F_o ATP synthase in the fermentative obligate anaerobic bacterium Clostridium pasteurianum was sequenced. It consisted of nine genes arranged in the order atpI(i), atpB(a), atpE(c), atpF(b), atpH(), atpA(), atpG(), atpD(ß), and atpC(), which was identical to that found in many bacteria. Reverse transcription-PCR confirmed the presence of the transcripts of all nine genes. The amount of ATPase activity in the membranes of C. pasteurianum was low compared to what has been found in many other bacteria. The F₁F_o complexes solubilized from membranes of C. pasteurianum and Escherichia coli had similar masses, suggesting similar compositions for the F₁F_o complexes from the two bacteria. Western blotting experiments with antibodies raised against the purified subunits of F₁F_o detected the presence of eight subunits, , ß, , , , a, b, and c, in the F₁F_o complex from C. pasteurianum. The F₁F_o complex from C. pasteurianum was activated by thiocyanate, cyanate, or sulfhydryl compounds; inhibited by sulfite, bisulfite, or bicarbonate; and had tolerance to inhibition by dicyclohexylcarbodiimide. The target of thiol activation of the F₁F_o complex from C. pasteurianum was F₁. Thiocyanate and sulfite were noncompetitive with respect to substrate Mg ATP but competitive with respect to each other. The F₁ and F_o parts of the F₁F_o complexes from C. pasteurianum and E. coli bound to each other, but the hybrid F₁F_o complexes were not functionally active.

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* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, A210 Life Sciences Building, University of Georgia, Athens, GA 30602. Phone: (706) 542-1086. Fax: (706) 542-2222. E-mail: adas{at}arches.uga.edu.

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Journal of Bacteriology, September 2003, p. 5527-5535, Vol. 185, No. 18
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.18.5527-5535.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

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