Possmayer, F E <br/><br/>
Covalent modification of the catalytic sites of the H(+)-ATPase from chloroplasts, CF(0)F(1), with 2-azido-[alpha-(32)P]ADP: modification of the catalytic site 2 (loose) and the catalytic site 3 (open) impairs multi-site, but not uni-site catalysis of both ATP synthesis and ATP hydrolysis.  [electronic resource] 

 -  Biochimica et biophysica acta  Jan 2000 
 - 77-98 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-3002 
<br/><br/><label>Standard No.: </label>10.1016/s0005-2728(99)00106-1  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Diphosphate--analogs & derivatives<br/>Adenosine Triphosphate--biosynthesis<br/>Azides--metabolism<br/>Catalytic Domain<br/>Chloroplasts--enzymology<br/>Hydrolysis<br/>Kinetics<br/>Liposomes<br/>Phosphorus Radioisotopes<br/>Photoaffinity Labels<br/>Protein Binding<br/>Proton-Translocating ATPases--metabolism