Why is the mechanical efficiency of F(1)-ATPase so high? (Q46356146)

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scientific article published in October 2000

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English	Why is the mechanical efficiency of F(1)-ATPase so high?	scientific article published in October 2000

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scholarly article

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Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

title

Why is the mechanical efficiency of F(1)-ATPase so high? (English)

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Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

author name string

G Oster

series ordinal

1

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Europe PubMed Central

PubMed publication ID

15254381

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21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

H Wang

series ordinal

2

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Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

publication date

1 October 2000

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Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

published in

Journal of Bioenergetics and Biomembranes

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stated in

Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

volume

32

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Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

issue

5

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stated in

Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

page(s)

459-469

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Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

cites work

ATP synthase--past and future

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactions

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

Stepping rotation of F1-ATPase visualized through angle-resolved single-fluorophore imaging

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Single kinesin molecules studied with a molecular force clamp

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Transcription against an applied force

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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On what makes the gamma subunit spin during ATP hydrolysis by F(1).

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

A structural change in the kinesin motor protein that drives motility

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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The Hsp70 and Hsp60 chaperone machines

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

Catalytic mechanism of F1-ATPase

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

Energy transduction in the F1 motor of ATP synthase

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Mechanism of energy coupling in the FOF1-ATP synthase: the uncoupling mutation, gammaM23K, disrupts the use of binding energy to drive catalysis

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Relevance of divalent cations to ATP-driven proton pumping in beef heart mitochondrial F0F1-ATPase

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Catalytic sites of Escherichia coli F1-ATPase

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Mg2+ coordination in catalytic sites of F1-ATPase

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Energy transduction in ATP synthase

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

Leading the procession: new insights into kinesin motors

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

The way things move: looking under the hood of molecular motor proteins

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Two-headed binding of a processive myosin to F-actin.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

The crystal structure of dimeric kinesin and implications for microtubule-dependent motility

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL.

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

Structure and function in GroEL-mediated protein folding

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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Structural model of F1-ATPase and the implications for rotary catalysis

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein friction exerted by motor enzymes through a weak-binding interaction

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Direct observation of the rotation of F1-ATPase

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

Adjustment of K' for the creatine kinase, adenylate kinase and ATP hydrolysis equilibria to varying temperature and ionic strength

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A rotary molecular motor that can work at near 100% efficiency

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The Entropic Cost of Bound Water in Crystals and Biomolecules

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

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inferred from PubMed ID database lookup

Catalytic site forms and controls in ATP synthase catalysis

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Biological applications of optical forces

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Rotation of F(1)-ATPase and the hinge residues of the beta subunit.

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Chemical mechanism of ATP synthase. Magnesium plays a pivotal role in formation of the transition state where ATP is synthesized from ADP and inorganic phosphate

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reverse engineering a protein: the mechanochemistry of ATP synthase

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis

1 reference

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The binding change mechanism for ATP synthase--some probabilities and possibilities

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/15254381

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Binding of the transition state analog MgADP-fluoroaluminate to F1-ATPase

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The force exerted by a single kinesin molecule against a viscous load

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Coordinated hydrolysis explains the mechanical behavior of kinesin.

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/15254381

retrieved

12 December 2020

based on heuristic

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Identifiers

DOI

10.1023/A:1005660807157

1 reference

stated in

Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

Dimensions Publication ID

1001911791

0 references

PubMed publication ID

15254381

1 reference

stated in

Europe PubMed Central

PubMed publication ID

15254381

retrieved

21 December 2017

reference URL

http://europepmc.org/abstract/MED/15254381

 

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