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

Component interactions and implications for complex formation in the multicomponent toluene 4-monooxygenase.

Luke A Moe1, Lea A McMartin, Brian G Fox

  • 1Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisconsin 53706-1544, USA

Biochemistry
|April 26, 2006
PubMed
Summary

Researchers studied protein interactions within the toluene 4-monooxygenase complex. They found specific binding between the effector protein (T4moD) and hydroxylase (T4moH) and ferredoxin (T4moC) components, suggesting a specialized electron transfer pathway.

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

Genome of an <i>Escherichia coli</i> engineered for improved control over polyhydroxyalkanoate monomer composition.

Microbiology resource announcements·2026
Same author

Proposal of metagenomic-origin LRA-5 as a precursor of active β-lactamases through Tyr69Gln and Val166Glu amino acid substitutions: a functional and structural analysis.

Antimicrobial agents and chemotherapy·2025
Same author

Multi-proteomics reveals integrated metabolic and regulatory networks for xylan catabolism in <i>Streptomyces</i> sp. SirexAA-E.

Microbiology spectrum·2025
Same author

Bacterial community structure associated with smokeless tobacco reference products under different storage conditions and durations.

Frontiers in public health·2025
Same author

MarK, a Novosphingobium aromaticivorans kinase required for catabolism of multiple aromatic monomers.

The Journal of biological chemistry·2025
Same author

Populus salicinoids: a thriving subfield in the omics era.

Tree physiology·2025

Area of Science:

  • Biochemistry
  • Enzyme kinetics
  • Protein-protein interactions

Background:

  • The toluene 4-monooxygenase complex is crucial for aromatic hydrocarbon degradation.
  • Understanding the subunit interactions is key to elucidating its catalytic mechanism.

Purpose of the Study:

  • To investigate the protein-protein interactions among the components of the toluene 4-monooxygenase complex.
  • To characterize the binding affinities and functional implications of these interactions.

Main Methods:

  • Preparation of a fluorophore-labeled T4moD using a tetraCys motif and biarsenical fluorescein.
  • Fluorescence anisotropy measurements to quantify binding interactions.
  • Analysis of interactions between T4moD, T4moH, T4moC, and T4moF.

Related Experiment Videos

Main Results:

  • T4moD directly binds to the hydroxylase component T4moH (K(D) = 83 nM) and the Rieske ferredoxin component T4moC (K(D) = 78 nM).
  • No direct binding was observed between T4moD and the NADH oxidoreductase component T4moF.
  • T4moF disrupted the T4moC-T4moD interaction, suggesting a specific complex formation.

Conclusions:

  • The findings suggest an intermediary electron transfer complex involving T4moC and T4moD, excluding T4moF.
  • Effector protein function specialization may involve specific interactions with [2Fe-2S] domains and hydroxylase components.