PMID:20214873
| Citation |
Friedrich, T and Hellwig, P Redox-induced conformational changes within the Escherichia coli NADH ubiquinone oxidoreductase (complex I): an analysis by mutagenesis and FT-IR spectroscopy. Biochim. Biophys. Acta 1797:659-63 |
|---|---|
| Abstract |
The proton-pumping NADH:ubiquinone oxidoreductase couples the transfer of electrons from NADH to ubiquinone with the translocation of protons across the membrane. This process is suggested to be accompanied by conformational changes of the enzyme that may be monitored by redox-induced FT-IR difference spectroscopy. Signals observed in the amide I range are partially attributed to local rearrangements that occur as an electrostatic response to the redox reactions of the FeS clusters. In addition, conformational changes can be reported that depend on pH and at the same time can be perturbed by site-directed mutagenesis of residue E67 on subunit B (the bacterial homologue of the mitochondrial PSST subunit). This residue is located in the vicinity of the cluster N2. Re-evaluating these previous data we here discuss a mechanism, by which the redox reaction of N2 induces conformational changes possibly leading to proton translocation. |
| Links |
PubMed Online version:10.1016/j.bbabio.2010.03.002 |
| Keywords |
Amino Acid Substitution; Electron Transport Complex I/chemistry; Electron Transport Complex I/genetics; Electron Transport Complex I/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Hydrogen-Ion Concentration; Mutagenesis, Site-Directed; Mutant Proteins/chemistry; Mutant Proteins/genetics; Mutant Proteins/metabolism; Oxidation-Reduction; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Spectroscopy, Fourier Transform Infrared |
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