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J. Biochem, 1970, Vol. 67, No. 2 157-174
© 1970 Japanese Biochemical Society

research-article

Phosphorylation of Bound Adenosine Monophosphate in the Electron Transfer Particle

TAKAYUKI OZAWA

Institute of Biochemistry, Faculty of Medicine, University of Nagoya Nagoya

  1. In the phosphorylating electron transfer particle, incorporated 32P by oxidative phosphorylation into the bound adenine nucleotides was found mainly in ADP and partly in ATP, 92% and 8% of the total 32Pe, respectively. Both kinetic and enzymatic analyses demonstrated that the bound ATP was terminally labelled and the labelling was due mainly to 32P1-ATP exchange reaction. The data indicated that the bound AMP was an earlier phosphoryl acceptor in the phosphorylation compartment.
  2. Approximately 65% of esterified 32P was found to be tightly bound with the phosphorylation compartment, being eluted from the particle neither by incubation for 30min at 30°C, nor by the digestion of "head" and "stalk" of the particle with Nagarse, but by the existence of exogenous adenine nucleotides. In contrast to 32Pe among the bound nucleotides, 32Pe appeared mainly in the extra-particular ATP with 76% of the total 32Pe. The presence of fluoride increased the percentage up to 85%. A phosphoryl transfer between the bound and exogenousADP was postulated.
  3. Treatment of the particle with EDTA suppressed both the amount of the bound nucleotide and that of the incorporated 32P down to about 4%. The externally added AMP to EDTA particle increased the amount of 32P incorporated into the bound ADP up to three fold without concomitant increase in that into the boundATP.
  4. Fluoride suppressed 32P incorporation into the bound ATP but accelerated the incorporation into the bound pyridine nucleotides and flavins. Percentage of 32P-labelled ADP to the total esterified 32P was not influenced by fluoride. It is postulated that a complicate equilibrium of high energy phosphoryl transfer exists in the bound nucleotides.


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