The Regulation of Pyruvate Dehydrogenase Activity in Pea Leaf Mitochondria (The Effect of Respiration and Oxidative Phosphorylation) | Zendy

Anthony L. Moore | Zendy; Joanna Gemel | Zendy; Douglas D. Randall | Zendy

Open Access

The Regulation of Pyruvate Dehydrogenase Activity in Pea Leaf Mitochondria (The Effect of Respiration and Oxidative Phosphorylation)

Author(s) -

Anthony L. Moore,

Joanna Gemel,

Douglas D. Randall

Publication year - 1993

Publication title -

plant physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 3.554

H-Index - 312

eISSN - 1532-2548

pISSN - 0032-0889

DOI - 10.1104/pp.103.4.1431

Subject(s) - oxidative phosphorylation , oligomycin , biochemistry , pyruvate dehydrogenase complex , pyruvate decarboxylation , mitochondrion , adenylate kinase , pyruvate dehydrogenase kinase , respiration , biology , uncoupling agents , oxoglutarate dehydrogenase complex , citric acid cycle , nadh dehydrogenase , dehydrogenase , respiratory chain , cellular respiration , pyruvate dehydrogenase phosphatase , metabolism , enzyme , protein subunit , atpase , botany , gene

The regulation of the pea (Pisum sativum) leaf mitochondrial pyruvate dehydrogenase complex by respiratory rate and oxidative phosphorylation has been investigated by measuring the respiratory activity, the redox poise of the quinone pool (Q-pool), and mitochondrial pyruvate dehydrogenase (mtPDC) activity under various metabolic conditions. It was found that, under state 4 conditions, mtPDC activity was unaffected by either the addition of succinate, 2-oxoglutarate, or glycine or the overall respiratory rate and redox poise of the Q-pool but was partially inhibited by NADH due to product inhibition. In the presence of ADP significant inactivation of PDC, which was sensitive to oligomycin, was observed with all substrates, apart from pyruvate, suggesting that inactivation was due to ATP formation. Inactivation of PDC by ADP addition was observed even in the presence of carboxyatractyloside, an inhibitor of the ATP/ADP translocator, suggesting that other mechanisms to facilitate the entry of adenylates, in addition to the adenylate carrier, must exist in plant mitochondria.

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