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Transhydrogenase and the anaerobic mitochondrial metabolism of adult Hymenolepis diminuta

Published online by Cambridge University Press:  21 September 2009

C. F. FIORAVANTI  and
K. P. VANDOCK
C. F. FIORAVANTI*
Affiliation:
Department of Biological Sciences, Bowling Green State University, Bowling Green Ohio 43403USA
K. P. VANDOCK
Affiliation:
Department of Biological Sciences, Bowling Green State University, Bowling Green Ohio 43403USA
*
*Corresponding author: Department of Biological Sciences, Bowling Green State University, Bowling Green Ohio 43402USA. Tel: (1) 419 372 2634. Fax: (1) 419 372 2024. E-mail: cfiorav@bgsu.edu
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Summary

The adult cestode, Hymenolepis diminuta, is essentially anaerobic energetically. Carbohydrate dissimilation results in acetate, lactate and succinate accumulation with succinate being the major end product. Succinate accumulation results from the anaerobic, mitochondrial, ‘malic’ enzyme-dependent utilization of malate coupled to ATP generation via the electron transport-linked fumarate reductase. A lesser peroxide-forming oxidase is apparent, however, fumarate reduction to succinate predominates even in air. The H. diminuta matrix-localized ‘malic’ enzyme is NADP-specific whereas the inner membrane (IM)-associated electron transport system prefers NADH. This dilemma is circumvented by the mitochondrial, IM-associated NADPH→NAD+ transhydrogenase in catalyzing hydride ion transfer from NADPH to NAD+ on the IM matrix surface. Hydride transfer is reversible and phospholipid-dependent. NADP+ reduction occurs as a non energy-linked and energy-linked reaction with the latter requiring electron transport NADH utilization or ATP hydrolysis. With NAD+ reduction, the cestode transhydrogenase also engages in concomitant proton translocation from the mitochondrial matrix to the intermembrane space and supports net ATP generation. Thus, the cestode NADPH→NAD+ system can serve not only as a metabolic connector, but an additional anaerobic phosphorylation site. Although its function(s) is unknown, a separate IM-associated NADH→ NAD+ transhydrogenation, catalyzed by the lipoamide and NADH dehydrogenases, is noted.

Keywords

Transhydrogenasemitochondriaanaerobic energeticsHymenolepis diminutacestodemetabolism
Type
Research Article
Information
Parasitology , Volume 137 , Special Issue 3: Development and applications of cestode and trematode laboratory models , March 2010 , pp. 395 - 410
Copyright
Copyright © Cambridge University Press 2009

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