Abstract
The ATP synthase from Escherichia coli is a prototype of the ATP synthases that are found in many bacteria, in the mitochondria of eukaryotes, and in the chloroplasts of plants. It contains eight different types of subunits that have traditionally been divided into F1, a water-soluble catalytic sector, and Fo, a membrane-bound ion transporting sector. In the current rotary model for ATP synthesis, the subunits can be divided into rotor and stator subunits. Several lines of evidence indicate that ε is one of the three rotor subunits, which rotate through 360 degrees. The three-dimensional structure of ε is known and its interactions with other subunits have been explored by several approaches. In light of recent work by our group and that of others, the role of ε in the ATP synthase from E. coli is discussed.
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Vik, S.B. What Is the Role of ε in the Escherichia coli ATP Synthase?. J Bioenerg Biomembr 32, 485–491 (2000). https://doi.org/10.1023/A:1005664908066
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DOI: https://doi.org/10.1023/A:1005664908066