4.5 Article

Energy conservation by Rhodothermus marinus respiratory complex I

期刊

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1797, 期 4, 页码 509-515

出版社

ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2010.01.020

关键词

Na-23-NMR; Complex I; Ion transport; NADH dehydrogenase; Proton; Sodium

资金

  1. FCT
  2. Projecto de Re-Equipamento Cientifico [REDE/1517/RMN/2005]
  3. Fundacao para a Ciencia e a Tecnologia [SFRH/BPD/34493/2006, SFRH/BD/25288/2005, POCI/BIA-PRO/58374/2004, POCI/QUI-BIQ/100302/2008, FCT-REEQ/336/BIO/2005]
  4. Parkinson Schweiz
  5. Fundação para a Ciência e a Tecnologia [POCI/BIA-PRO/58374/2004, SFRH/BPD/34493/2006, SFRH/BD/25288/2005] Funding Source: FCT

向作者/读者索取更多资源

A sodium ion efflux, together with a Proton influx and an inside-positive AT, was observed during NADH-respiration by Rhodothermus marinus membrane vesicles. Proton translocation was monitored by fluorescence spectroscopy and sodium ion transport by Na-23-NMR spectroscopy. Specific inhibitors Of complex I (rotenone) and of the dioxygen reductase (KCN) inhibited the proton and the sodium ion transport, but the KCN effect was totally reverted by the addition of menaquinone analogues, indicating that both transports were catalyzed by complex I. We concluded that the coupling ion of the system is the proton and that neither the catalytic reaction nor the establishment of the delta-pH are dependent on sodium, but the presence of sodium increases proton transport, Moreover, studies of NADH oxidation at different sodium concentrations and of proton and sodium transport activities allowed us to propose a model for the mechanism of complex I in which the presence of two different energy coupling sites is suggested. (C) 2010 Elsevier B.V. All rights reserved.

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