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Showing 1 to 17 of 17 for “"NADH:ubiquinone oxidoreductase"”.
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Biochemical Studies of the Sodium -Translocating NADH:ubiquinone Oxidoreductase
… cofactor to take electrons from the substrate, NADH, and that the electrons then flow to the 2Fe-2S center.
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Structural and functional studies of mitochondrial NADH:ubiquinone oxidoreductase (complex I)
NADH:ubiquinone oxidoreductase (complex I) is the largest and most complicated enzyme in the mitochondrial electron transfer chain. It catalyses the oxidation of NADH and the reduction of ubiquinone, coupled to the translocation of protons across the mitochondrial inner membrane, maintaining the …
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Investigations of the mechanism of mitochondrial complex I by electron cryomicroscopy
… electrons through a series of membrane-embedded oxidoreductase proteins known as the electron transport chain (ETC). The first enzyme in the ETC is complex I (NADH:ubiquinone oxidoreductase). Complex I oxidises NADH in the matrix, reduces ubiquinone in the inner membrane, and couples the energy …
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Cryo-electron microscopy studies on ovine mitochondrial complex I
… I. Mitochondrial complex I (also known as NADH:ubiquinone oxidoreductase) is one of the central enzymes in the oxidative phosphorylation pathway. It couples electron transfer between NADH and ubiquinone to proton translocation across the inner mitochondrial membrane, contributing to …
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The Role of Mitochondria in Oxygen Sensing of the Ductus Arteriosus and Fetal Pulmonary Arteries
… normoxic DASMC. Among genes in ETC Complex I, NADH:Ubiquinone oxidoreductase core subunit S2 (NDUFS2) was uniquely downregulated by oxygen. 2) Knockdown of NDUFS2 reduced DASMC acute oxygen responsiveness without bioenergetic inhibition. 3) Rabbit DA and PA have unique proteomes, with …
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Therapeutic Approaches to Insulin Resistance and Type 2 Diabetes
… I of the mitochondrial respiratory chain (NADH:ubiquinone oxidoreductase), leading to a likely increase in the AMP to ATP ratio and the consequential activation of the cellular energy regulator, AMPK. This in turn stimulated the signalling pathway which enhanced the incorporation of the …
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Role of oxidative stress in photoreceptor degeneration
… were treated with a mitochondrially targeted ubiquinone derivative (MitoQ), which is a powerful antioxidant, to try and slow the rate of retinal degeneration. MitoQ was administered orally during pregnancy and for an extended postnatal period and uptake, toxicity, breeding behaviour and …
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Using molecular approaches to understand Complex I deficiency in mouse models
Complex I (NADH:ubiquinone oxidoreductase), a major electron entry point to the mitochondrial respiratory chain, couples electron transfer from NADH to ubiquinone to proton pumping across the mitochondrial inner membrane, and generates the proton motive force that drives ATP synthesis and transport …
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Structural Studies into the Mechanism and Organisation of Mammalian Respiratory Complex I
Respiratory complex I (NADH:ubiquinone oxidoreductase) is the major entry point of electrons into the electron transport chain and couples its redox activity with proton pumping across the inner mitochondrial membrane, thus contributing to the proton motive force which drives ATP synthesis. With …
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Developing mouse complex I as a model system: structure, function and implications in mitochondrial diseases.
Complex I (NADH:ubiquinone oxidoreductase), located in the mitochondrial inner membrane, is a major electron entry point to the respiratory chain. It couples the energy released from electron transfer (from NADH to ubiquinone) to the concomitant pumping of protons across the membrane, to generate …
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Mutagenesis investigations into proton transfer pathways and control points in respiratory complex I
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a large multi-subunit membrane protein that uses the energy from electron transfer from NADH to ubiquinone to transport four protons across an energy transducing membrane. The protons contribute to building the proton-motive force that …
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Studies on assembly and genetic variation in mitochondrial respiratory complex I
Complex I (NADH:ubiquinone oxidoreductase) couples electron transfer to proton translocation across the inner mitochondrial membrane, to drive the synthesis of ATP. Its distinctive L-shaped structure comprises 45 subunits, encoded by both the mitochondrial and nuclear genomes, which are assembled …
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Investigating the rate-limiting step of mitochondrial complex I catalysis
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a key enzyme in metabolism and is the least understood protein in the mitochondrial electron transfer chain (ETC). It couples the energy released from NADH oxidation and ubiquinone (Q) reduction to the translocation of four protons across …
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Paracoccus denitrificans as a model system for studying the mechanism of respiratory complex I
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a crucial metabolic enzyme that couples the free energy released from NADH oxidation and ubiquinone reduction to the translocation of four protons across an energy-transducing membrane, contributing to the proton motive force used to …
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Structure-function studies of respiratory complex I from Paracoccus denitrificans using membrane mimetics
Respiratory complex I (NADH:ubiquinone oxidoreductase) is a crucial metabolic enzyme that couples the free energy released from NADH oxidation and ubiquinone reduction to translocate four protons across energy-transducing membranes, contributing to the proton motive force that powers oxidative …
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Cryo-EM studies of substrate and inhibitor binding to mammalian respiratory complex I
Mammalian respiratory complex I (NADH:ubiquinone oxidoreductase) is an intricate multi-subunit, energy-transducing membrane protein that is essential for aerobic energy metabolism and NADH/NAD⁺ homeostasis. It couples the energy released from NADH oxidation and ubiquinone (Q) reduction to pump four …
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Mutagenese des nuo-Operons von Escherichia coli
Die protonenpumpende NADH:Ubichinon Oxidoreduktase (Komplex I) koppelt den Transfer der Elektronen des NADH über ein Flavinmononukleotid und neun Eisen-Schwefel (Fe/S)-Zentren auf ein Chinon mit der Translokation von vier Protonen über die Membran. Aufgrund fehlender Strukturdaten und seines …