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Substrate–Protein Interactions of Type II NADH:Quinone Oxidoreductase from Escherichia coli
Citation key doi:10.1021/acs.biochem.6b00070
Author Salewski, Johannes and Batista, Ana P. and Sena, Filipa V. and Millo, Diego and Zebger, Ingo and Pereira, Manuela M. and Hildebrandt, Peter
Pages 2722-2734
Year 2016
DOI 10.1021/acs.biochem.6b00070
Journal Biochemistry
Volume 55
Number 19
Note PMID: 27109164
Abstract Type II NADH:quinone oxidoreductases (NDH-2s) are membrane proteins involved in respiratory chains and responsible for the maintenance of NADH/NAD+ balance in cells. NDH-2s are the only enzymes with NADH dehydrogenase activity present in the respiratory chain of many pathogens, and thus, they were proposed as suitable targets for antimicrobial therapies. In addition, NDH-2s were also considered key players for the treatment of complex I-related neurodegenerative disorders. In this work, we explored substrate–protein interaction in NDH-2 from Escherichia coli (EcNDH-2) combining surface-enhanced infrared absorption spectroscopic studies with electrochemical experiments, fluorescence spectroscopy assays, and quantum chemical calculations. Because of the specific stabilization of substrate complexes of EcNDH-2 immobilized on electrodes, it was possible to demonstrate the presence of two distinct substrate binding sites for NADH and the quinone and to identify a bound semiprotonated quinol as a catalytic intermediate.
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