BIOMAT Database Logo BIOMAT Database Logo

Chemomechanical coupling of human mitochondrial F1-ATPase motor. 2014

Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
1] Faculty of Science and Engineering, Waseda University, Shinjuku-ku, Tokyo, Japan. [2] ATP Synthesis Regulation Project, International Research Project (ICORP), Japan Science and Technology Corporation (JST), Miraikan, Koto-ku, Tokyo, Japan. [3] Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta, Yokohama, Japan.

The rotary motor enzyme F1-ATPase (F1) is a catalytic subcomplex of FoF1-ATP synthase that produces most of the ATP in respiring cells. Chemomechanical coupling has been studied extensively for bacterial F1 but very little for mitochondrial F1. Here we report ATP-driven rotation of human mitochondrial F1. A rotor-shaft γ-subunit in the stator α3β3 ring rotates 120° per ATP with three catalytic steps: ATP binding to one β-subunit at 0°, inorganic phosphate (Pi) release from another β-subunit at 65° and ATP hydrolysis on the third β-subunit at 90°. Rotation is often interrupted at 90° by persistent ADP binding and is stalled at 65° by a specific inhibitor azide. A mitochondrial endogenous inhibitor for FoF1-ATP synthase, IF1, blocks rotation at 90°. These features differ from those of bacterial F1, in which both ATP hydrolysis and Pi release occur at around 80°, demonstrating that chemomechanical coupling angles of the γ-subunit are tuned during evolution.

UI MeSH Term Description Entries
D008928 Mitochondria Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed) Mitochondrial Contraction,Mitochondrion,Contraction, Mitochondrial,Contractions, Mitochondrial,Mitochondrial Contractions
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D006180 Proton-Translocating ATPases Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane. ATP Dependent Proton Translocase,ATPase, F0,ATPase, F1,Adenosinetriphosphatase F1,F(1)F(0)-ATPase,F1 ATPase,H(+)-Transporting ATP Synthase,H(+)-Transporting ATPase,H(+)ATPase Complex,Proton-Translocating ATPase,Proton-Translocating ATPase Complex,Proton-Translocating ATPase Complexes,ATPase, F(1)F(0),ATPase, F0F1,ATPase, H(+),Adenosine Triphosphatase Complex,F(0)F(1)-ATP Synthase,F-0-ATPase,F-1-ATPase,F0F1 ATPase,F1-ATPase,F1F0 ATPase Complex,H(+)-ATPase,H(+)-Transporting ATP Synthase, Acyl-Phosphate-Linked,H+ ATPase,H+ Transporting ATP Synthase,H+-Translocating ATPase,Proton-Translocating ATPase, F0 Sector,Proton-Translocating ATPase, F1 Sector,ATPase Complex, Proton-Translocating,ATPase Complexes, Proton-Translocating,ATPase, H+,ATPase, H+-Translocating,ATPase, Proton-Translocating,Complex, Adenosine Triphosphatase,Complexes, Proton-Translocating ATPase,F 0 ATPase,F 1 ATPase,F0 ATPase,H+ Translocating ATPase,Proton Translocating ATPase,Proton Translocating ATPase Complex,Proton Translocating ATPase Complexes,Proton Translocating ATPase, F0 Sector,Proton Translocating ATPase, F1 Sector,Triphosphatase Complex, Adenosine
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006868 Hydrolysis The process of cleaving a chemical compound by the addition of a molecule of water.
D000255 Adenosine Triphosphate An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter. ATP,Adenosine Triphosphate, Calcium Salt,Adenosine Triphosphate, Chromium Salt,Adenosine Triphosphate, Magnesium Salt,Adenosine Triphosphate, Manganese Salt,Adenylpyrophosphate,CaATP,CrATP,Manganese Adenosine Triphosphate,MgATP,MnATP,ATP-MgCl2,Adenosine Triphosphate, Chromium Ammonium Salt,Adenosine Triphosphate, Magnesium Chloride,Atriphos,Chromium Adenosine Triphosphate,Cr(H2O)4 ATP,Magnesium Adenosine Triphosphate,Striadyne,ATP MgCl2
D001386 Azides Organic or inorganic compounds that contain the -N3 group. Azide
D012399 Rotation Motion of an object in which either one or more points on a line are fixed. It is also the motion of a particle about a fixed point. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Clinorotation,Clinorotations,Rotations
D055162 Biocatalysis The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.

Related Publications

Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Chemomechanical coupling of F1-ATPase under hydrolysis conditions.
January 2012, Biophysics (Nagoya-shi, Japan),
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Tight Chemomechanical Coupling of the F1 Motor Relies on Structural Stability.
July 2020, Biophysical journal,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
On chemomechanical coupling of the F(1)-ATPase molecular motor.
July 2009, Biochimica et biophysica acta,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Is F1-ATPase a Rotary Motor with Nearly 100% Efficiency? Quantitative Analysis of Chemomechanical Coupling and Mechanical Slip.
May 2019, Nano letters,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Chemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation.
February 2004, Nature structural & molecular biology,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Simple mechanism whereby the F1-ATPase motor rotates with near-perfect chemomechanical energy conversion.
August 2015, Proceedings of the National Academy of Sciences of the United States of America,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Visualization of mitochondrial coupling factor F1(ATPase) by freeze-drying.
March 1979, Cell biophysics,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Coupling factor activity of the purified pea mitochondrial F1-ATPase.
December 1985, Biochimica et biophysica acta,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Generic maps of optimality reveal two chemomechanical coupling regimes for motor proteins: from F1-ATPase and kinesin to myosin and cytoplasmic dynein.
January 2018, Integrative biology : quantitative biosciences from nano to macro,
Toshiharu Suzuki, and Kazumi Tanaka, and Chiaki Wakabayashi, and Ei-ichiro Saita, and Masasuke Yoshida
Elastic coupling power stroke mechanism of the F1-ATPase molecular motor.
May 2018, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!