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Am J Physiol Cell Physiol (July 21, 2004). doi:10.1152/ajpcell.00286.2004
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Submitted on June 16, 2004
Accepted on July 15, 2004

Decreased affinity for oxygen of cytochrome c oxidase in Leigh syndrome caused by SURF1 mutation

Petr Pecina1, Erich Gnaiger2, Jiri Zeman3, Ewa Pronicka4, and Josef Houstek1*

1 Department of Bioenergetics, Institute of Physiology and Center for Integrated Genomics, Academy of Sciences of the Czech Republic, Prague, Czech Republic
2 Department of Transplant Surgery, D. Swarovski Research Laboratory, University Hospital Innsbruck, Innsbruck, Tyrolia, Austria
3 Department of Pediatrics, 1st Medical Faculty, Charles University, Prague, Czech Republic
4 Department of Metabolic Diseases, Children's Memorial Health Hospital, Warsaw, Poland

* To whom correspondence should be addressed. E-mail: houstek{at}biomed.cas.cz.

Mutations in SURF1 gene prevent synthesis of cytochrome c oxidase (COX) - specific assembly protein and result in a fatal neurological disorder, Leigh syndrome. Because this severe COX deficiency presents with hardly detectable changes of cellular respiratory rates at normoxic conditions, we analyzed the respiratory response to low oxygen in cultured fibroblasts harboring SURF1 mutations using high-resolution respirometry. The oxygen kinetics was quantified by the p50 (the pO2 at half-maximal respiration rate) in intact coupled cells and in digitonin-permeabilized uncoupled cells. In both cases, the p50 in patients was 2.1- and 3.3-fold elevated, respectively, indicating decreased affinity of COX to oxygen. These results suggest that at physiologically low intracellular pO2 the depressed oxygen affinity may in vivo lead to limitations of respiration resulting in impaired energy provision in Leigh syndrome patients.




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