Bioelectrochemistry (Amsterdam, Netherlands), 2023-06, Vol.151, p.108379
2023
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Details
- Autor(en) / Beteiligte
- Titel
- Mutating the environment of heme b 595 of E. coli cytochrome bd-I oxidase shifts its redox potential by 200 mV without inactivating the enzyme
- Ist Teil von
- Bioelectrochemistry (Amsterdam, Netherlands), 2023-06, Vol.151, p.108379
- Ort / Verlag
- Netherlands
- Erscheinungsjahr
- 2023
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Cytochrome bd-I catalyzes the reduction of oxygen to water with the aid of hemes b , b and d. Here, effects of a mutation of E445, a ligand of heme b and of R448, hydrogen bonded to E445 are studied electrochemically in the E. coli enzyme. The equilibrium potential of the three hemes are shifted by up to 200 mV in these mutants. Strikingly the E445D and the R448N mutants show a turnover of 41 ± 2 % and 20 ± 4 %, respectively. Electrocatalytic studies confirm that the mutants react with oxygen and bind and release NO. These results point towards the ability of cytochrome bd to react even if the electron transfer is less favorable.
- Sprache
- Englisch
- Identifikatoren
- eISSN: 1878-562XTitel-ID: cdi_pubmed_primary_36736178
- Format
- –
- Schlagworte
- Cytochromes - genetics, Cytochromes - metabolism, Electron Transport, Electron Transport Chain Complex Proteins - genetics, Electron Transport Chain Complex Proteins - metabolism, Escherichia coli - metabolism, Escherichia coli Proteins - genetics, Escherichia coli Proteins - metabolism, Oxidation-Reduction, Oxidoreductases - genetics, Oxidoreductases - metabolism, Oxygen - metabolism