title: Rotating proton pumping ATPases: subunit/subunit interactions and thermodynamics.
abstract: In this article, we discuss single molecule observation of rotational catalysis by E. coli ATP synthase (F-ATPase) using small gold beads. Studies involving a low viscous drag probe showed the stochastic properties of the enzyme in alternating catalytically active and inhibited states. The importance of subunit interaction between the rotor and the stator, and thermodynamics of the catalysis are also discussed. "Single Molecule Enzymology" is a new trend for understanding enzyme mechanisms in biochemistry and physiology.
authors: Department of Biochemistry, Faculty of Pharmaceutical Sciences, Iwate Medical University, and Futai Special Laboratory, Yahaba, Iwate, Japan. nakanim@iwate-med.ac.jp
authors: Mayumi
authors: M
authors: Nakanishi-Matsui
authors: Mizuki
authors: M
authors: Sekiya
authors: Masamitsu
authors: M
authors: Futai
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D020134:Catalytic Domain; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D006046:Gold / Q000737:chemistry; D006868:Hydrolysis; D056004:Molecular Dynamics Simulation; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry* / Q000378:metabolism; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism; D011522:Protons; D012399:Rotation; D013816:Thermodynamics
chemical_list: D029968:Escherichia coli Proteins; D020409:Molecular Motor Proteins; D021122:Protein Subunits; D011522:Protons; D006046:Gold; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases