Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Substrate-induced conformational change in bacterial complex I.

Aygun A Mamedova1, Peter J Holt, Joe Carroll

  • 1Medical Research Council Dunn Human Nutrition Unit, Wellcome Trust/Medical Research Council Building, Cambridge CB2 2XY, United Kingdom.

The Journal of Biological Chemistry
|March 24, 2004
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Assembly of the catalytic module and the rotor of human ATP synthase.

The EMBO journal·2026
Same author

Structure of E. coli twin-arginine translocase (Tat) complex with bound cargo.

Molecular cell·2026
Same author

Treatments for metastatic non-small cell lung cancer: a pathways pilot with systematic review, evidence synthesis and economic model.

Health technology assessment (Winchester, England)·2026
Same author

Supplementary search methods versus bibliographic database searching to identify studies and study reports.

The Cochrane database of systematic reviews·2025
Same author

Author Correction: SCAF1 drives the compositional diversity of mammalian respirasomes.

Nature structural & molecular biology·2025
Same author

Clinical and cost-effectiveness of clopidogrel resistance genotype testing after ischaemic stroke or transient ischaemic attack: a systematic review and economic model.

Health technology assessment (Winchester, England)·2024
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
Same journal

PAX8 controls proximal tubule epithelial identity and stress response through epigenetic modification of distal regulatory elements.

The Journal of biological chemistry·2026
See all related articles

Substrate binding to respiratory complex I (NADH-ubiquinone oxidoreductase) induces conformational changes. NAD(P)H binding causes a more open structure in the complex, impacting both its peripheral arm and membrane domain.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Respiratory complex I (NADH-ubiquinone oxidoreductase) is crucial for cellular energy production.
  • The mechanism linking electron transfer and proton pumping remains unclear, with conformational changes proposed as a key factor.

Purpose of the Study:

  • To investigate the influence of substrates on the conformation of purified Escherichia coli complex I.
  • To elucidate the structural dynamics of complex I upon substrate binding.

Main Methods:

  • Cross-linking experiments using various reagents to probe subunit proximity.
  • Electron microscopy, including single-particle analysis, to visualize structural changes.
  • Proteolysis assays to assess subunit accessibility.

Related Experiment Videos

Main Results:

  • NAD(P)H binding, unlike NAD+ binding, reduced cross-linking between hydrophilic subunits, indicating increased mobility.
  • Subunit NuoB, associated with the N2 iron-sulfur cluster, was identified as a highly mobile component.
  • NAD(P)H binding enhanced proteolysis of subunit NuoG.
  • Electron microscopy revealed a more open conformation of the peripheral arm and, unexpectedly, the membrane domain upon NADH binding.

Conclusions:

  • Substrate binding induces significant conformational changes in respiratory complex I.
  • The peripheral arm and membrane domain undergo structural rearrangements upon NAD(P)H binding, suggesting a mechanism for energy transduction.