AMP photophosphorylation and binding by chloroplasts.
Stoichiometric amounts of chloroplast thylakoids photophosphorylate free AMP to tightly bound ADP. Free ADP is a poor competitor for this AMP photoreaction, which saturates below 16 micronAMP. The inhibitor, diadenosine pentaphosphate, abolishes AMP photophosphorylation, and inhibits dark ADP binding. Taken together, these data imply that this photoreaction involves the high affinity nucleotide binding site(s) of chloroplast coupling factor CF1, and that little mixing with free nucleotides occurs.
D000227:Adenine Nucleotides / Q000494:pharmacology; D000244:Adenosine Diphosphate / Q000378:metabolism; D000249:Adenosine Monophosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D002736:Chloroplasts / Q000378:metabolism*; D006593:Hexokinase / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008027:Light; D010710:Phosphates / Q000378:metabolism; D010785:Photophosphorylation; D006180:Proton-Translocating ATPases / Q000378:metabolism
D000227:Adenine Nucleotides; D010710:Phosphates; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D006593:Hexokinase; D006180:Proton-Translocating ATPases