ATP synthase motor components: Proposal and animation of two dynamic models for stator function

David J. Blum, Young Hee Ko, Sangjin Hong, David A Rini, Peter L Pedersen

Research output: Contribution to journalArticle

Abstract

Recent research indicates that ATP synthases (F0F1) contain two distinct nanomotors, one an electrochemically driven proton motor contained within F0 that drives an ATP hydrolysis-driven motor (F1) in reverse during ATP synthesis. This is depicted in recent models as involving a series of events in which each of the three αβ pairs comprising F1 is induced via a centrally rotating subunit (γ) to undergo the sequential binding changes necessary to synthesize ATP (binding change mechanism). Stabilization of this rotary process (i.e., to minimize "wobble" of F1) is provided in current models by a peripheral stalk or "stator" that has recently been shown to extend from near the bottom of the ATP synthase molecule to the very top of F1. Although quite elegant, these models envision the stator as fixed during ATP synthesis, i.e., bound to only a single αβ pair. This is despite the fact that the binding change mechanism views each αβ pair as going through the same sequential order of conformational changes which demonstrate a chemical equivalency among them. For this reason, we propose here two different dynamic models for stator function during ATP synthesis. Both models have been designed to maintain chemical equivalency among the three αβ pairs during ATP synthesis and both have been animated.

Original languageEnglish (US)
Pages (from-to)801-807
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume287
Issue number4
DOIs
StatePublished - Oct 5 2001

Fingerprint

Animation
Stators
Dynamic models
Adenosine Triphosphate
Protons
Hydrolysis
Stabilization
Molecules
Research

Keywords

  • ATP synthase
  • ATP synthesis
  • Bioenergetics
  • F-ATPase
  • Mitochondria
  • Molecular machines
  • Molecular motors
  • Nanomotors
  • Nanotechnology
  • Oxidative phosphorylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

ATP synthase motor components : Proposal and animation of two dynamic models for stator function. / Blum, David J.; Ko, Young Hee; Hong, Sangjin; Rini, David A; Pedersen, Peter L.

In: Biochemical and Biophysical Research Communications, Vol. 287, No. 4, 05.10.2001, p. 801-807.

Research output: Contribution to journalArticle

Blum, David J. ; Ko, Young Hee ; Hong, Sangjin ; Rini, David A ; Pedersen, Peter L. / ATP synthase motor components : Proposal and animation of two dynamic models for stator function. In: Biochemical and Biophysical Research Communications. 2001 ; Vol. 287, No. 4. pp. 801-807.
@article{279de3261a044a02846688c83502d0aa,
title = "ATP synthase motor components: Proposal and animation of two dynamic models for stator function",
abstract = "Recent research indicates that ATP synthases (F0F1) contain two distinct nanomotors, one an electrochemically driven proton motor contained within F0 that drives an ATP hydrolysis-driven motor (F1) in reverse during ATP synthesis. This is depicted in recent models as involving a series of events in which each of the three αβ pairs comprising F1 is induced via a centrally rotating subunit (γ) to undergo the sequential binding changes necessary to synthesize ATP (binding change mechanism). Stabilization of this rotary process (i.e., to minimize {"}wobble{"} of F1) is provided in current models by a peripheral stalk or {"}stator{"} that has recently been shown to extend from near the bottom of the ATP synthase molecule to the very top of F1. Although quite elegant, these models envision the stator as fixed during ATP synthesis, i.e., bound to only a single αβ pair. This is despite the fact that the binding change mechanism views each αβ pair as going through the same sequential order of conformational changes which demonstrate a chemical equivalency among them. For this reason, we propose here two different dynamic models for stator function during ATP synthesis. Both models have been designed to maintain chemical equivalency among the three αβ pairs during ATP synthesis and both have been animated.",
keywords = "ATP synthase, ATP synthesis, Bioenergetics, F-ATPase, Mitochondria, Molecular machines, Molecular motors, Nanomotors, Nanotechnology, Oxidative phosphorylation",
author = "Blum, {David J.} and Ko, {Young Hee} and Sangjin Hong and Rini, {David A} and Pedersen, {Peter L}",
year = "2001",
month = "10",
day = "5",
doi = "10.1006/bbrc.2001.5634",
language = "English (US)",
volume = "287",
pages = "801--807",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - ATP synthase motor components

T2 - Proposal and animation of two dynamic models for stator function

AU - Blum, David J.

AU - Ko, Young Hee

AU - Hong, Sangjin

AU - Rini, David A

AU - Pedersen, Peter L

PY - 2001/10/5

Y1 - 2001/10/5

N2 - Recent research indicates that ATP synthases (F0F1) contain two distinct nanomotors, one an electrochemically driven proton motor contained within F0 that drives an ATP hydrolysis-driven motor (F1) in reverse during ATP synthesis. This is depicted in recent models as involving a series of events in which each of the three αβ pairs comprising F1 is induced via a centrally rotating subunit (γ) to undergo the sequential binding changes necessary to synthesize ATP (binding change mechanism). Stabilization of this rotary process (i.e., to minimize "wobble" of F1) is provided in current models by a peripheral stalk or "stator" that has recently been shown to extend from near the bottom of the ATP synthase molecule to the very top of F1. Although quite elegant, these models envision the stator as fixed during ATP synthesis, i.e., bound to only a single αβ pair. This is despite the fact that the binding change mechanism views each αβ pair as going through the same sequential order of conformational changes which demonstrate a chemical equivalency among them. For this reason, we propose here two different dynamic models for stator function during ATP synthesis. Both models have been designed to maintain chemical equivalency among the three αβ pairs during ATP synthesis and both have been animated.

AB - Recent research indicates that ATP synthases (F0F1) contain two distinct nanomotors, one an electrochemically driven proton motor contained within F0 that drives an ATP hydrolysis-driven motor (F1) in reverse during ATP synthesis. This is depicted in recent models as involving a series of events in which each of the three αβ pairs comprising F1 is induced via a centrally rotating subunit (γ) to undergo the sequential binding changes necessary to synthesize ATP (binding change mechanism). Stabilization of this rotary process (i.e., to minimize "wobble" of F1) is provided in current models by a peripheral stalk or "stator" that has recently been shown to extend from near the bottom of the ATP synthase molecule to the very top of F1. Although quite elegant, these models envision the stator as fixed during ATP synthesis, i.e., bound to only a single αβ pair. This is despite the fact that the binding change mechanism views each αβ pair as going through the same sequential order of conformational changes which demonstrate a chemical equivalency among them. For this reason, we propose here two different dynamic models for stator function during ATP synthesis. Both models have been designed to maintain chemical equivalency among the three αβ pairs during ATP synthesis and both have been animated.

KW - ATP synthase

KW - ATP synthesis

KW - Bioenergetics

KW - F-ATPase

KW - Mitochondria

KW - Molecular machines

KW - Molecular motors

KW - Nanomotors

KW - Nanotechnology

KW - Oxidative phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=0035812687&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035812687&partnerID=8YFLogxK

U2 - 10.1006/bbrc.2001.5634

DO - 10.1006/bbrc.2001.5634

M3 - Article

C2 - 11573932

AN - SCOPUS:0035812687

VL - 287

SP - 801

EP - 807

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -