Mitochondrial function and critical temperature in the Antarctic bivalve, Laternula elliptica

Thermal sensitivities of maximum respiration and proton leakage were compared in gill mitochondria of the Antarctic bivalve Laternula elliptica for an assessment of the contribution of mitochondrial mechanisms to limiting temperature tolerance. Proton leakage was measured as the oxygen consumption rate during blockage of oxidative phosphorylation (state IV respiration + oligomycin). The maximum capacity of NADP dependent mitochondrial isocitrate dehydrogenase (IDH) was investigated as part of a proposed mitochondrial substrate cycle provoking proton leakage by the action of transhydrogenase. State III and IV + respiration rose exponentially with temperature. Thermal sensitivities of proton leakage and IDH were unusually high, in accordance with the hypothesis that H(+) leakage is an enzyme catalysed process with IDH being involved. In contrast to proton leakage, state III respiration exhibited an Arrhenius break temperature at 9 degrees C, visible as a drop in thermal sensitivity close to, but still above the critical temperature of the species (3-6 degrees C). Progressive uncoupling of mitochondria led to a drop in RCR values and P/O ratios at high temperature. The same discontinuity as for state III respiration was found for the activity of mitochondrial IDH suggesting that this enzyme may influence the thermal control of mitochondrial respiration. In general, the high thermal sensitivity of proton leakage may cause an excessive rise in mitochondrial oxygen demand and a decreased efficiency of oxidative phosphorylation. This may exceed the whole animal capacity of oxygen uptake and distribution by ventilation and circulation and set a thermal limit, characterized by the transition to anaerobic metabolism. (C) 1999 Elsevier Science Inc. All rights reserved

Details

Publication status:
Published
Author(s):
Authors: Pörtner, Hans O., Hardewig, Iris, Peck, Lloyd S.

On this site: Lloyd Peck
Date:
1 January, 1999
Journal/Source:
Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology / 124
Page(s):
179-189
Digital Object Identifier (DOI):
https://doi.org/10.1016/S1095-6433(99)00105-1