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Title: Energy-linked adenosine diphosphate accumulation by corn mitochondria. General characteristics and effect of inhibitors

Journal Article · · Plant Physiol.; (United States)
DOI:https://doi.org/10.1104/pp.64.2.276· OSTI ID:5518423

Corn mitochondria show respiration-linked net accumulation of (/sup 3/H)ADP in the presence of phosphate and magnesium, especially if the formation of ATP is blocked with oligomycin. Inhibition of ADP-ATP exchange by carboxyatractyloside also activates ADP accumulation, and addition of carboxyatractyloside or palmitoyl-coenzyme A to oligomycin-blocked mitochondria produces additional ADP uptake. With carboxyatractyloside the accumulated ADP is phosphorylated to ATP. With oligomycin, only a little ATP is formed. Millimolar concentrations of ADP are required for maximum uptake, and the K/sub m/ (3.77 millimolar) for ADP translocation is independent of whether oligomycin or carboxyatractyloside is used. This is not true for ADP concentrations in the 0.05 to 0.25 millimolar range. Accumulated (/sup 3/H)ADP rapidly exchanges with unlabeled AMP, ADP, or ATP, but not with other diphosphate nucleotides or 2 millimolar substrate anions. (/sup 3/H)AMP is not accumulated, but (/sup 3/H)ATP is accumulated to about one-half the extent of (/sup 3/H)ADP. Tricarboxylate substrates inhibit ADP net uptake, and inhibition by citrate is competitive with K/sub i/ = 10 millimolar. The evidence suggests the presence of a pathway, carboxyatractyloside-insensitive and different from the translocase, which operates to maintain adenine nucleotides in the matrix.

Research Organization:
Univ. of Illinois at Urbana-Champaign, IL (United States)
DOE Contract Number:
EY-76-S-02-0790
OSTI ID:
5518423
Journal Information:
Plant Physiol.; (United States), Vol. 64:2
Country of Publication:
United States
Language:
English