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

Methane monooxygenase hydroxylase and B component interactions.

Jingyan Zhang1, Bradley J Wallar, Codrina V Popescu

  • 1Department of Biochemistry, Molecular Biology and Biophysics and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, Minnesota 55455, USA.

Biochemistry
|March 1, 2006
PubMed
Summary

The soluble methane monooxygenase regulatory component (MMOB) interacts with the hydroxylase component (MMOH) via a specific surface, primarily through electrostatic interactions. This interaction is crucial for regulating substrate access to the MMOH active site.

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

A piperidinyl amide compound enhances Ca<sup>2+</sup> signaling in cardiomyocytes by increasing activity of Ca<sup>2+</sup> pump.

Biophysical reports·2026
Same author

Development of activators for SERCA2a for heart failure treatments.

European journal of medicinal chemistry·2025
Same author

Large-scale high-throughput screen for cardiac ryanodine receptor targeted therapeutics.

The Journal of biological chemistry·2025
Same author

A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Multicenter Histology Image Integration and Multiscale Deep Learning for Machine Learning-Enabled Pediatric Sarcoma Classification.

medRxiv : the preprint server for health sciences·2025
Same author

Tyrosine-Mediated Static and Dynamic Quenching of a Receptor Tyrosine Kinase Biosensor Reveals Inhibitor Binding Modes and Kinase Conformations.

ACS chemical biology·2025

Area of Science:

  • Biochemistry
  • Enzymology
  • Protein-protein interactions

Background:

  • Soluble methane monooxygenase (MMO) is a crucial enzyme for methane oxidation.
  • The MMO system comprises hydroxylase (MMOH) and regulatory (MMOB) components.
  • Understanding the MMOH-MMOB interaction is key to elucidating MMO regulation.

Purpose of the Study:

  • To map the interaction surface between MMOB and MMOH.
  • To investigate the role of electrostatic interactions in MMOH-MMOB complex formation.
  • To characterize the kinetics and thermodynamics of the MMOH-MMOB binding reaction.

Main Methods:

  • Site-directed mutagenesis to introduce cysteine residues in MMOB.
  • Spin labeling with MSL and fluorescence labeling with BADAN and 1,5-IAEDANS.

Related Experiment Videos

  • Electron paramagnetic resonance (EPR) spectroscopy and fluorescence spectroscopy.
  • Steady-state kinetic assays and affinity measurements.

    • Main Results:

    • A specific interaction surface on MMOB was identified, characterized by hydrophilic and charged residues.
    • The MMOH-MMOB complex is stabilized by electrostatic interactions, sensitive to pH and ionic strength.
    • Fluorescence studies revealed a two-step binding process, possibly involving conformational changes.
    • MMOB binding affinity is significantly reduced upon MMOH reduction.

    Conclusions:

    • The study defines the MMOB-MMOH interaction interface and highlights the importance of electrostatic forces in complex stability.
    • The findings suggest a regulatory mechanism involving conformational changes upon binding, influencing substrate access.
    • This work provides insights into the intricate regulation of methane oxidation by soluble MMO.