• NADH Dehydrogenase

    SURFE²R N1: Application of 100 µM NADH results in a current over the mitochondrial membrane, where Complex I and III are expressed

NADH Dehydrogenase - NADH : Ubiquinone Oxidoreductase

H+ or Na+-translocating NADH dehydrogenase (NDH), a member of the Na+ transporting Mrp superfamily 

In mammals, the enzyme contains 44 separate water soluble peripheral membrane proteins, which are anchored to the integral membrane constituents.

It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10). In eukaryotes, it is located in the inner mitochondrial membrane. It is one of the "entry enzymes" of cellular respiration or oxidative phosphorylation in the mitochondria and contains to the electron transport chain (ETC) complex I. The reaction catalyzed by complex I is:
NADH + H+ + CoQ + 4H+in→ NAD+ + CoQH2 + 4H+out
In this process, the complex translocates four protons across the inner membrane per molecule of oxidized NADH, helping to build the electrochemical potential difference used to produce ATP.

Data and Applications

Respiratory Chain Complex I and III - Current Over Mitochondrial Membrane

Surfer RC complexI III traceIcon N1   SURFE2R N1 data and applications:

In the respiratory chain Complex I and III, oxidation of NADH leads to transport of 4 protons across the membrane. The electrons are transferred to cytochrome c. Because of the electron leakage to oxygen, both complex are the main sites of production of harmful superoxide. In these experiments using the SURFE2R N1, application of 100µM NADH results in a current over the mitochondrial membrane, where Complex I and III are expressed.



2013 - Measuring Interference of Drug-Like Molecules with the Respiratory Chain: Toward the Early Identification of Mitochondrial Uncouplers in Lead Finding

Icon 96SE   SURFE²R N96 (predesessor model of SURFE²R 96SE) publication in Assay and Drug Development Technologies (2013)

Stock U., Matter H., Diekert K., Dörner W., Dröse S., Licher T.

a.      P-bond hydrolysis driven transporters

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