Participation of epsilonADP and epsilonATp in the reactions of oxidative phosphorylation in rat liver mitochondria.
The 1,N6-ethenoadenine nucleotide analogs epsilonADP and epsilonATP, contrary to recent findings (1), are shown to be unable to penetrate the inner mitochondrial membrane of intact rat liver mitochondria and can not be used as substrates by the respiratory chain enzymes in oxidative phosphorylation. On the other hand, these analogs are able to participate in transphosphorylation reactions, being good substrates for mitochondrial phosphotransferases located in the intermembrane space, such as nucleosidediphosphate kinase and adenylate kinase.
Bârzu
O
O
Department of Biochemistry, Medical and Pharmaceutical Institute, Cluj-Napoca, Romania.
Kiss
L
L
Bojan
O
O
Niac
G
G
Mantsch
H H
HH
D000244:Adenosine Diphosphate / Q000031:analogs & derivatives* / Q000378:metabolism* / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism* / Q000494:pharmacology; D000818:Animals; D002384:Catalysis / Q000187:drug effects; D019069:Cell Respiration / Q000187:drug effects; D006868:Hydrolysis / Q000187:drug effects; D008274:Magnesium / Q000494:pharmacology; D008930:Mitochondria, Liver / Q000187:drug effects / Q000378:metabolism*; D010085:Oxidative Phosphorylation / Q000187:drug effects; D051381:Rats
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D008274:Magnesium