The photosynthetic F1-α3β3 and α1β1 catalytic core complexes |
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Authors: | Zippora Gromet-Elhanan Maxim Sokolov |
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Institution: | (1) Department of Biochemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel |
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Abstract: | Minimal photosynthetic catalytic F1() core complexes, containing equimolar ratios of the and subunits, were isolated from membrane-bound spinach chloroplast CF1 and Rhodospirillum rubrum chromatophore RrF1. A CF1-33 hexamer and RrF1-11 dimer, which were purified from the respective F1() complexes, exhibit lower rates and different properties from their parent F1-ATPases. Most interesting is their complete resistance to inhibition by the general F1 inhibitor azide and the specific CF1 inhibitor tentoxin. These inhibitors were earlier reported to inhibit multisite, but not unisite, catalysis in all sensitive F1-ATPases and were therefore suggested to block catalytic site cooperativity. The absence of this typical property of all F1-ATPases in the 11 dimer is consistant with the view that the dimer contains only a single catalytic site. The 33 hexamer contains however all F1 catalytic sites. Therefore the observation that CF1-33 can bind tentoxin and is stimulated by it suggests that the F1 subunit, which is required for obtaining inhibition by tentoxin as well as azide, plays an important role in the cooperative interactions between the F1-catalytic sites.Abbreviations CF0F1
chloroplast F0F1
- CF1
chloroplast F1
- CF1
chloroplast F1 subunit
- CF1
chloroplast F1 subunit
- CF1()
a complex containing equal amounts of the CF1 and subunits
- MF1
mitochondrial F1
- RrF0F1
Rhodospirillum rubrum F0F1
- RrF1
R. rubrum F1
- RrF1
R. rubrum F1 subunit
- RrF1
R. rubrum F1 subunit
- RrF1()
a complex containing equal amounts of the RrF1 and subunits
- Rubisco
Ribulose-1,5-bisphosphate carboxylase
- TF1
thermophilic bacterium PS3 F1 |
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Keywords: | ATP-synthase catalytic site cooperativity F1-ATPase rhodospirillum rubrum chromatophores spinach chloroplasts tentoxin |
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