caa a22 4500 397558651 CHVBK 20180308164810.0 cr unu---uuuuu 161202e199611 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021510 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021510 The Heterogeneous Interaction of Substoichiometric TNP-ATP and F1 -ATPase from Escherichia coli [Elektronische Daten] [Eiro Muneyuki, Toru Hisabori, Takeshi Sasayama, Katsura Mochizuki, Masasuke Yoshida] The interactions of substoichiometric TNP-ATP and F1-ATPase from Escherichia coil (EF1) were examined and compared with those in the case of mitochondrial F1-ATPase (MF1) and F1-ATPase from thermophilic Bacillus PS3 (TF1). EF, hydrolyzed substoichiometric TNP-ATP faster than TF1 or MF1, although some 20% of the TNP-ATP remained unhydrolyzed even in the presence of excess chase ATP. The affinity of the catalytic site of EF1 for the product, TNP-ADP1 was weaker than that of TF1 or MF1, and the TNP-ADP was readily released upon addition of excess ATP. The amplitude of the difference absorption spectrum induced by binding of TNP-AT(D)P to EF1 was smaller than that of MF1 or TF1 under similar experimental conditions. When an excess amount of TNP-ATP was added to EF1 and the change of the difference spectrum was measured, the shape of the difference spectrum of the ATP-replaceable fraction was very similar to that in the case of binding of TNP-ATP to the isolated β subunit of TF1, indicating that the rapidly replaceable fraction of bound TNP-ATP was actually at the catalytic site and most of the non-replaceable portion was bound at noncatalytic sites. Weaker affinity of the catalytic site for TNP-ATP may account for the heterogeneous binding and hydrolysis under the conditions described in this paper. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence Escherichia coli nationallicence F1-ATPase nationallicence nucleotide binding nationallicence TNP-ATP nationallicence uni-site catalysis nationallicence Muneyuki Eiro Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut Hisabori Toru Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut Sasayama Takeshi Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut Mochizuki Katsura Department of Chemistry, Yokohama City University Seto, Yokohama 236 aut Yoshida Masasuke Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut The Journal of Biochemistry Oxford University Press 120/5(1996-11), 940-945 0021-924X 120:5<940 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021510 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021510 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Muneyuki Eiro Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut NATIONALLICENCE 700 1- Hisabori Toru Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut NATIONALLICENCE 700 1- Sasayama Takeshi Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut NATIONALLICENCE 700 1- Mochizuki Katsura Department of Chemistry, Yokohama City University Seto, Yokohama 236 aut NATIONALLICENCE 700 1- Yoshida Masasuke Research Laboratory of Resources Utilization, Tokyo Institute of Technology Nagatsuta 4259, Midori-ku, Yokohama 226 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/5(1996-11), 940-945 0021-924X 120:5<940 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford