title: Elastic rotation of Escherichia coli F(O)F(1) having ε subunit fused with cytochrome b(562) or flavodoxin reductase.
abstract: Intra-molecular rotation of FOF1 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 FOF1 with the ε subunit connected to a globular protein [cytochrome b562 (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.
authors.affiliation: Department of Bioscience, Nagahama Institute of Bioscience and Technology, Nagahama, Shiga 526-0829, Japan.
authors.forename: Hideyuki
authors.initials: H
authors.lastname: Oka
authors.affiliation: Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Yahaba, Iwate 028-3694, Japan.
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Hosokawa
authors.affiliation: Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Yahaba, Iwate 028-3694, Japan.
authors.forename: Mayumi
authors.initials: M
authors.lastname: Nakanishi-Matsui
authors.affiliation: Department of Biochemistry, University of Western Ontario, London, Ontario N6A 5C1, Canada.
authors.forename: Stanley D
authors.initials: SD
authors.lastname: Dunn
authors.affiliation: Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, Yahaba, Iwate 028-3694, Japan.
authors.forename: Masamitsu
authors.initials: M
authors.lastname: Futai
authors.affiliation: Department of Bioscience, Nagahama Institute of Bioscience and Technology, Nagahama, Shiga 526-0829, Japan. Electronic address: a_iwamoto@nagahama-i-bio.ac.jp.
authors.forename: Atsuko
authors.initials: A
authors.lastname: Iwamoto-Kihara
mesh_terms: D019677:Artificial Gene Fusion; D003573:Cytochrome b Group / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D050939:Gene Fusion; D008958:Models, Molecular; D009247:NADH, NADPH Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D003573:Cytochrome b Group; D029968:Escherichia coli Proteins; D021122:Protein Subunits; C017850:cytochrome b562, E coli; D009247:NADH, NADPH Oxidoreductases; C116041:flavodoxin NADPH oxidoreductase; D006180:Proton-Translocating ATPases
keywords: ATP synthase; Elastic rotation; Energy coupling; F(O)F(1); Molecular motor; ε Subunit