Abstract
Escherichia coli ATP synthase has eight subunits and functions through transmission of conformational changes between subunits. Extensive mutational analyses identified essential residues for catalysis and conformation transmission. Pseudorevertant studies revealed that β/α and β/γ subunits interactions are important for the energy coupling between catalysis and H+ translocation. In this article, we discuss mechanism of catalysis and energy coupling based on our recent mutation studies.
Original language | English |
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Pages (from-to) | 177-183 |
Number of pages | 7 |
Journal | Acta Physiologica Scandinavica, Supplement |
Volume | 163 |
Issue number | 643 |
Publication status | Published - Jan 1 1998 |
Externally published | Yes |
Keywords
- ATP synthase
- Mutagenesis
- Pseudorevertant
- Rotation
- Rotational catalysis
ASJC Scopus subject areas
- Physiology