title: A biological molecular motor, proton-translocating ATP synthase: multidisciplinary approach for a unique membrane enzyme.
abstract: Proton-translocating ATP synthase (F(o)F(1)) synthesizes ATP from ADP and phosphate, coupled with an electrochemical proton gradient across the biological membrane. It has been established that the rotation of a subunit assembly is an essential feature of the enzyme mechanism and that F(o)F(1) can be regarded as a molecular motor. Thus, experimentally, in the reverse direction (ATP hydrolysis), the chemical reaction drives the rotation of a gammaepsilonc(10-14) subunit assembly followed by proton translocation. We discuss our very recent results regarding subunit rotation in Escherichia coli F(o)F(1) with a combined biophysical and mutational approach.
authors.affiliation: Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, CREST (Core Research for Evolutional Science and Technology) of Japan Science and Technology Corporation, Ibaraki, Osaka 567-0047, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Sambongi
authors.forename: I
authors.initials: I
authors.lastname: Ueda
authors.forename: Y
authors.initials: Y
authors.lastname: Wada
authors.forename: M
authors.initials: M
authors.lastname: Futai
mesh_terms: D019943:Amino Acid Substitution; D025243:Bacterial Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000378:metabolism; D021122:Protein Subunits; D018892:Proton-Motive Force; D013816:Thermodynamics
chemical_list: D020409:Molecular Motor Proteins; D021122:Protein Subunits; D025243:Bacterial Proton-Translocating ATPases