skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Elastic rotation of Escherichia coli F{sub O}F{sub 1} having ε subunit fused with cytochrome b{sub 562} or flavodoxin reductase

Journal Article · · Biochemical and Biophysical Research Communications
 [1]; ;  [2];  [3];  [2];  [1]
  1. Department of Bioscience, Nagahama Institute of Bioscience and Technology, Nagahama, Shiga 526-0829 (Japan)
  2. Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Yahaba, Iwate 028-3694 (Japan)
  3. Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1 (Canada)

Highlights: • Intra-molecular rotation of F{sub O}F{sub 1} ATP synthase was observed using a small bead probe. • Carboxyl-terminus of the ε subunit was fused to cytochrome b{sub 562} or flavodoxin reductase. • The F{sub O}F{sub 1} showed continual rotation with similar rate to the wild-type enzyme. • The intra-molecular rotation is flexible and elastic. - Abstract: Intra-molecular rotation of F{sub O}F{sub 1} ATP synthase enables cooperative synthesis and hydrolysis of ATP. In this study, using a small gold bead probe, we observed fast rotation close to the real rate that would be exhibited without probes. Using this experimental system, we tested the rotation of F{sub O}F{sub 1} with the ε subunit connected to a globular protein [cytochrome b{sub 562} (ε-Cyt) or flavodoxin reductase (ε-FlavR)], which is apparently larger than the space between the central and the peripheral stalks. The enzymes containing ε-Cyt and ε-FlavR showed continual rotations with average rates of 185 and 148 rps, respectively, similar to the wild type (172 rps). However, the enzymes with ε-Cyt or ε-FlavR showed a reduced proton transport. These results indicate that the intra-molecular rotation is elastic but proton transport requires more strict subunit/subunit interaction.

OSTI ID:
22416376
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 446, Issue 4; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English

Similar Records

Effects of mutations in the {beta} subunit hinge domain on ATP synthase F{sub 1} sector rotation: Interaction between Ser 174 and Ile 163
Journal Article · Fri Jan 11 00:00:00 EST 2008 · Biochemical and Biophysical Research Communications · OSTI ID:22416376

Molecular insights on cytochrome c and nucleotide regulation of apoptosome function and its implication in cancer
Journal Article · Wed Jan 01 00:00:00 EST 2020 · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · OSTI ID:22416376

Mitochondrial ATP synthase complex: interaction of its F/sub 1/ adenosinetriphosphatase moiety with the heavy atom iodine
Journal Article · Tue Jun 30 00:00:00 EDT 1987 · Biochemistry; (United States) · OSTI ID:22416376