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

Active site electronic structure and dynamics during metalloenzyme catalysis.

Oded Kleifeld1, Anatoly Frenkel, Jan M L Martin

  • 1Department of Structural Biology, The Weizmann Institute of Science, Rehovot 76100, Israel.

Nature Structural Biology
|January 14, 2003
PubMed
Summary

This study reveals the dynamic structural changes of zinc ions in alcohol dehydrogenase during catalysis. Understanding these zinc enzyme mechanisms offers new insights into cellular processes.

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

Tumor-draining lymph nodes in ovarian cancer lack germinal centers but harbor tumor-reactive memory B cells clonally linked to intra-tumoral B cells.

Immunity·2026
Same author

Toward an Affordable Density-Based Measure for the Quality of a Coupled Cluster Calculation.

The journal of physical chemistry. A·2026
Same author

It's time to rethink academic innovation: why technology transfer offices can't do it alone.

Nature biotechnology·2026
Same author

Altered ECM deposition and cell adhesion signaling in a human cortical organoid model of fragile X syndrome.

Molecular brain·2026
Same author

Development of Local Natural Orbital Arbitrary Order Coupled Cluster Methods and Assessment through Connected Quadruples.

The journal of physical chemistry. A·2026
Same author

Coupling between Thermochemical Contributions of Subvalence Correlation and of Higher-Order Post-CCSD(T) Correlation Effects─A Step toward "W5 Theory".

The journal of physical chemistry. A·2026

Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Zinc-dependent enzymes are crucial for numerous cellular functions.
  • Elucidating the reaction mechanisms of these enzymes is challenging due to the spectroscopic silence of the zinc ion.

Purpose of the Study:

  • To investigate the dynamic behavior and structural alterations of the active site zinc ion in bacterial alcohol dehydrogenase during catalysis.
  • To provide novel mechanistic insights into alcohol dehydrogenase function.

Main Methods:

  • Utilized time-resolved X-ray absorption spectroscopy.
  • Employed pre-steady state kinetics.
  • Integrated computational quantum chemistry.

Main Results:

Related Experiment Videos

  • Observed dynamic changes in the coordination number and structure of the catalytic zinc ion during substrate turnover.
  • Detected concomitant alterations in metal-ligand bond distances.
  • Correlated structural changes with the effective charge of the zinc ion.

Conclusions:

  • Catalytic zinc sites exhibit significant flexibility during enzymatic reactions.
  • The study provides new mechanistic understanding of alcohol dehydrogenase catalysis.
  • Highlights the utility of combining spectroscopic, kinetic, and computational methods for studying metalloenzymes.