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

Raman difference spectroscopic studies of the myosin S1.MgADP.vanadate complex

H Deng1, J Wang, R H Callender

  • 1Department of Physics, City College of the City University of New York 10031, USA.

Biochemistry
|August 7, 1998
PubMed
Summary

Raman spectroscopy reveals vanadate distortions in myosin S1.MgADP.Vi, suggesting a concerted SN2-like phosphotransfer mechanism. Strategic water positioning at the active site is crucial for myosin ATPase activity.

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

The elongated ciliated cells derived from nasal polyps are distinctly different from ciliated cells in different parts of the nasal mucosa.

Rhinology·2026
Same author

Intrinsically chiral exciton polaritons in an atomically-thin semiconductor.

Nature communications·2026
Same author

Average and Heterogeneous Associations between Secondhand Smoking and Tooth Loss.

Journal of dental research·2026
Same author

[Evaluation of the embryonic developmental toxicity of 3, 4-dinitrofurazanfuroxan using embryonic stem cell test model].

Zhonghua lao dong wei sheng zhi ye bing za zhi = Zhonghua laodong weisheng zhiyebing zazhi = Chinese journal of industrial hygiene and occupational diseases·2026
Same author

[Subacute toxicity study of triethylenediammonium perchlorate ammonium complex salt in rats].

Zhonghua lao dong wei sheng zhi ye bing za zhi = Zhonghua laodong weisheng zhiyebing zazhi = Chinese journal of industrial hygiene and occupational diseases·2025
Same author

[Surveillance of the population density of adult <i>Aedes albopictus</i> in Guangdong Province from 2018 to 2023].

Zhongguo xue xi chong bing fang zhi za zhi = Chinese journal of schistosomiasis control·2025

Area of Science:

  • Biochemistry
  • Biophysics
  • Enzymology

Background:

  • Myosin S1.MgADP.Vi complex serves as a transition-state analogue for myosin-catalyzed phosphotransfer.
  • Vanadate's nonbridging V--O bonds are key to understanding this reaction mechanism.

Purpose of the Study:

  • To investigate the structural changes of vanadate within the myosin S1.MgADP.Vi complex using Raman spectroscopy.
  • To elucidate the role of active site water in the myosin ATPase catalytic cycle.

Main Methods:

  • Raman difference spectroscopy to obtain spectra of vanadate in solution and in the myosin complex.
  • Empirical relationships to determine vanadate bond order and length.
  • Normal-mode and ab initio calculations to analyze structural conformations and interactions.

Related Experiment Videos

Main Results:

  • Distinct Raman spectra were observed for vanadate in solution (870 cm-1) versus the myosin complex (870, 844, 829 cm-1).
  • Vanadate bond order and length changed upon binding to myosin, indicating structural distortions.
  • A water molecule at the active site forms a V-O(H2) bond, influencing vanadate frequencies.

Conclusions:

  • The myosin S1.MgADP.Vi complex exhibits a distorted, near-planar vanadate moiety.
  • Strategic positioning of an active site water molecule is critical for myosin ATPase activity.
  • The myosin-catalyzed phosphotransfer reaction likely proceeds via a concerted (SN2-like) mechanism.