INV-1 Discovery of ATP motor and its mechanism(Invited lecture 1)
スポンサーリンク
概要
- 論文の詳細を見る
All living organisms on the earth rely solely on a single molecule as an energy currency, ATP (adenosine triphosphate). This small molecule supports nearly all the cellular activities that require energy, and our body synthesizes roughly as much ATP every day as our body weight. In the biological world, ATP synthesis is certainly the most prevalent chemical reaction and the enzyme, ATP synthase, responsible for most of this task, is one of the most ubiquitous, abundant proteins on the earth. ATP synthase uses physical rotation of its own subunits as a step of catalysis -a novel mechanism, different from any other known enzymes. Rotation is not a favourite motion in living organisms; there is no animal with wheels, no bird with a propeller, and no fish with a screw. On a molecular scale, besides ATP synthase only bacterial flagella are known as a rotary motor. The crystal structures of the main part of ATP synthase show in atomic detail how the appearance of this world tiniest motor made of protein is remarkably reminiscent of the man-made motors. The driving force that spins ATP synthase is gradient of hydrogen ion concentration across membranes that in turn is made by respiration (burning the food) or by sunshine. We have video-imaged the rotary motion of ATP synthase that spins as fast as several hundreds revolutions per second. The mechanism of the motor is completely different from the man-made motor. ATP synthase is two-particle structure connected with a common rotary shaft. The flow of hydrogen ions through the lower particle drives the rotation of the central rotor that then forces upper particle to make the bending motion for synthesis of ATP. Imagine billions of billion rotary motors are spinning in our body, day and night, without rest. When the motors stop, we die.
- 超音波エレクトロニクスの基礎と応用に関するシンポジウム運営委員会の論文
- 2005-11-16
著者
-
Yoshida Masasuke
Chemical Resources Laboratory, Tokyo Institute of Technology
-
Yoshida Masasuke
Chemical Resources Laboratory Tokyo Institute Of Technology
-
Yoshida Masasuke
Chemical Research Laboratory Tokyo Institute Of Technology
関連論文
- 2P100 Structural Characterization of Sup35 Amyloid Fibrils(31. Protein folding and misfolding (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P284 The behavior of F_1 motor in the presense of the uniform external torque applied with electrorotation(9. Molecular motor (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- Kinetic Mechanism of Quinol Oxidation by Cytochrome bd Studied with Ubiquinone-2 Analogs
- 2P-190 Effects of sodium dodecyl sulfate on F_1-ATPase Effects of sodium dodecyl sulfate on F_1-ATPase(The 46th Annual Meeting of the Biophysical Society of Japan)
- 2P-180 γsubunitにねじれを加えたF_1-ATPase変異体による軸の役割の解明(分子モーター(2),第46回日本生物物理学会年会)
- 2P156 Solid-State NMR Measurement of H^+-ATP Synthase Subunit c-ring Reconstituted into DMPC bilayers(34. Membrane protein,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P254 Conformations and chemical states of F_1-ATPase during rotation(9. Molecular motor (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P-163 αサブユニット変異体を導入したハイブリッドF_1の非対称な回転(分子モーター(1),第46回日本生物物理学会年会)
- 3P-131 ATP駆動の回転においてV-ATPaseは特徴的なステップ状回転を示す(分子モーター(3),第46回日本生物物理学会年会)
- 2P211 Mechanical Modulation of ATP binding affinity and ATP hydrolysis/synthesis equilibrium of F_1-ATPase(37. Molecular motor (II),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P528 Development of the Single Molecule Imaging System of the F_0 Motor(26. Single molecule biophysics,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- 1P529 Rotation rate of F_1-ATPase increases from 10 to 2000 over the temperature range of 5°-65℃(26. Single molecule biophysics,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)
- INV-1 Discovery of ATP motor and its mechanism(Invited lecture 1)
- Probing Dynamics and Conformational Change of the GroEL-GroES Complex by ^C NMR Spectroscopy
- Thiol modulation of the chloroplast ATP synthase is dependent on the energization of thylakoid membranes
- On-Chip Single-Cell Observation Assay for Propagation Dynamics of Yeast Sup35 Prionlike Proteins