Identification of subunits required for the catalytic activity of the F1-ATPase |
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Authors: | Zippora Gromet-Elhanan |
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Affiliation: | (1) Department of Biochemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel |
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Abstract: | F1() complexes containing equimolar ratios of the and subunits have been shown to function as active ATPases, whereas individually isolated and subunits show no real ATPase activity. These results indicate that the single-copy subunits are not required for F1-ATPase activity. The minimal F1()-core complexes exhibit, however, lower rates and some different properties from those of their parent whole F1 or 33 complexes. It is therefore concluded that for obtaining a full spectrum of the characteristic functional properties of an F1-ATPase the presence of the F1- subunit is also required. The implications of these findings on the subunit location of both catalytic and noncatalytic nucleotide binding sites is discussed. |
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Keywords: | F1-ATPase ATP synthase catalytic subunits nucleotide binding sites cooperative kinetics multisite catalysis azide tentoxin |
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