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

Nitric oxide synthase structure and electron transfer

P R Ortiz de Montellano1, C Nishida, I Rodriguez-Crespo

  • 1Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA. ortiz@cgl.ucsf.edu

Drug Metabolism and Disposition: the Biological Fate of Chemicals
|December 23, 1998
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

Instrument flight to the inner ear.

Science robotics·2018
Same author

The accuracy of image-based safety analysis for robotic cochlear implantation.

International journal of computer assisted radiology and surgery·2018
Same author

Patient's experience with subcutaneous and oral methotrexate for the treatment of rheumatoid arthritis.

BMC musculoskeletal disorders·2016
Same author

[12 years of Computer-Aided Surgery around the Head : Developments in surgical planning and simulation from a Bern perspective].

HNO·2016
Same author

Inhibition of plasmin attenuates murine acute graft-versus-host disease mortality by suppressing the matrix metalloproteinase-9-dependent inflammatory cytokine storm and effector cell trafficking.

Leukemia·2014
Same author

Dynamic chromosome reorganization in the osprey ( Pandion haliaetus , Pandionidae, Falconiformes): relationship between chromosome size and the chromosomal distribution of centromeric repetitive DNA sequences.

Cytogenetic and genome research·2014
Same journal

High-level expression of full-length human CYP2E1 in Escherichia coli: Comparison of full-length human CYP2E1 to truncated counterpart shows enhanced association with redox partners.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

Construction of a curated human pharmacokinetics database for molecular fragment analysis and machine learning applications.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

Finding the dispersion number (D<sub>N</sub>) of the dispersion model from perfused rat and human liver studies.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

Role of organic anion transporting polypeptides in pancreatic statin disposition and islet cell function in mice.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

The regulatory potential of cytochrome P450-adrenodoxin interactions: Insights toward understanding redox partner regulation in drug metabolizing enzymes.

Drug metabolism and disposition: the biological fate of chemicals·2026
Same journal

Enantioselective determination of methylone and its major phase 1 metabolites in various biological matrices and stereochemical stability of methylone enantiomers.

Drug metabolism and disposition: the biological fate of chemicals·2026
See all related articles

Nitric oxide synthases (NOS) use tetrahydrobiopterin as an electron donor for oxygen activation. Electron transfer rates, particularly from the flavin domain, critically determine NOS enzyme activity.

Area of Science:

  • Biochemistry
  • Enzymology

Background:

  • Nitric oxide synthases (NOS) share catalytic and spectroscopic similarities with cytochromes P450.
  • A key distinction is NOS enzymes' requirement for tetrahydrobiopterin (BH4).

Purpose of the Study:

  • To elucidate the role of tetrahydrobiopterin in nitric oxide synthase function.
  • To investigate the mechanism of electron transfer and its impact on catalytic turnover.

Main Methods:

  • Spectroscopic and chemical studies to determine cofactor binding.
  • Analysis of enzyme chimeras with exchanged reductase domains.
  • Catalytic activity assays.

Main Results:

  • Tetrahydrobiopterin binds near the heme prosthetic group, acting as a transient electron donor for oxygen activation.

Related Experiment Videos

  • The flavin domain's electron-donating capacity is a critical determinant of NOS catalytic turnover rate.
  • Electron transfer kinetics within and between flavin and heme domains significantly influence enzyme activity.

    • Conclusions:

    • Tetrahydrobiopterin plays a crucial role in facilitating rapid electron transfer for oxygen activation in NOS.
    • The efficiency of electron delivery from the flavin domain is a rate-limiting factor for NOS catalysis.