- PII
- 10.31857/S0026365624030119-1
- DOI
- 10.31857/S0026365624030119
- Publication type
- Status
- Published
- Authors
- Volume/ Edition
- Volume 93 / Issue number 3
- Pages
- 346-350
- Abstract
- In bacteria F-type ATPase (F-ATPase) plays a key role in bioenergetics and couples ATP synthesis/hydrolysis with the transport of ions (H+ or Na+) across the membrane. The ion specificity of the enzyme is determined by the amino acid sequence of subunits c and а. Here, we introduced several mutations (7 in subunit c and 6 in subunit a) into F-ATPase of thermophilic bacterium Bacillus sp. PS3 in order to change the ion specificity of the enzyme from proton to sodium. The mutations did not affect the ATPase activity of the enzyme, but led to loss of proton conductivity and impaired the binding of subunit a to the c-subunit oligomer, rather than changed the ion specificity.
- Keywords
- роторные АТФазы F-АТФазы F0F1 ионная специфичность трансмембранный перенос ионов мутагенез
- Date of publication
- 15.05.2024
- Year of publication
- 2024
- Number of purchasers
- 0
- Views
- 36
References
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