2006
DOI: 10.1074/jbc.m603442200
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The Redox-Bohr Group Associated with Iron-Sulfur Cluster N2 of Complex I

Abstract: Proton pumping respiratory complex I (NADH:ubiquinone oxidoreductase) is a major component of the oxidative phosphorylation system in mitochondria and many bacteria. In mammalian cells it provides 40% of the proton motive force needed to make ATP. Defects in this giant and most complicated membrane-bound enzyme cause numerous human disorders. Yet the mechanism of complex I is still elusive. A group exhibiting redox-linked protonation that is associated with iron-sulfur cluster N2 of complex I has been proposed… Show more

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Cited by 74 publications
(69 citation statements)
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“…Since the FMN is located almost 90 Å from the membrane plane (16), it is virtually impossible to construct any FMN-catalyzed proton-translocating loop mechanism. The alternative might be that redox-dependent conformational coupling (13,(45)(46)(47)(48) is operating together with a direct ubiquinone reduction-associated loop mechanism which may result in the observed overall H + /e stoichiometry of 4. The redox-dependent nucleotide binding change as reported here may be a part of such a conformational coupling.…”
Section: Discussionmentioning
confidence: 99%
“…Since the FMN is located almost 90 Å from the membrane plane (16), it is virtually impossible to construct any FMN-catalyzed proton-translocating loop mechanism. The alternative might be that redox-dependent conformational coupling (13,(45)(46)(47)(48) is operating together with a direct ubiquinone reduction-associated loop mechanism which may result in the observed overall H + /e stoichiometry of 4. The redox-dependent nucleotide binding change as reported here may be a part of such a conformational coupling.…”
Section: Discussionmentioning
confidence: 99%
“…The assembly of the complex was usually quite normal (Kashani-Poor et al 2001b;Grgic et al 2004). One mutation (H226M) led to a 80 mV decrease of the midpoint potential of the N2 signal and an apparent loss of the pH dependence of its midpoint potential (Zwicker et al 2006). Other mutations in the 49-kDa subunit and a series mutations in the PSST subunit, some very close to its Fe-S cluster assumed by these authors to be cluster N2 (Zickermann et al 2009), did not induce any qualitative changes in the EPR signal of N2 (or any of the other signals) of the mutant enzyme ).…”
Section: Spin Concentrations Of the Individual Epr Signalsmentioning
confidence: 99%
“…Several techniques have been described for monitoring cell respiration in a multiwell format using oxygen-dependent fluorescence quenching to monitor the oxygen concentration in the medium. These techniques either operate at steady-state, where oxygen consumption is balanced by inward diffusion of oxygen [63], or measure oxygen depletion in a sealed chamber [64,65]. Although these can be used to monitor or compare basal cell respiration rates, their low time resolution and the limited ability to make additions during the run preclude them from being used for sophisticated respiration assays.…”
Section: Fluxes: Mitochondrial Proton Current (Respiration Rate) In Cmentioning
confidence: 99%