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

Oxygen diffusion through horseradish peroxidase.

J E Brunet1, C Jullian, D M Jameson

  • 1Instituto de Quimica, Universidad Catolica de Valparaiso, Chile.

Photochemistry and Photobiology
|April 1, 1990
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

Spectroscopic studies of the interaction of 3-(2-thienyl)-[1,2,3]triazolo[1,5-a]pyridine with 2,6-dimethyl-β-cyclodextrin and ctDNA.

Organic & biomolecular chemistry·2016
Same author

Amino acid profiles and liposomes: Their role as chemosensory information carriers in the marine environment.

Journal of chemical ecology·2013
Same author

A method for on-line background subtraction in frequency domain fluorometry.

Journal of fluorescence·2013
Same author

Guanidinium chloride-induced spectral perturbations of 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid confound interpretation of data on molten globule states.

Analytical biochemistry·2011
Same author

ESR, electrochemical and cyclodextrin-inclusion studies of triazolopyridyl pyridyl ketones and dipyridyl ketones derivatives.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy·2008
Same author

Activation of dynamin II by POPC in giant unilamellar vesicles: a two-photon fluorescence microscopy study.

Journal of protein chemistry·2002
Same journal

Geometrical isomerization of hydroxycinnamic acid under UV-light: Structural plasticity as a driver of metabolite complexity.

Photochemistry and photobiology·2026
Same journal

Photochemistry of CryB from Rhodobacter sphaeroides.

Photochemistry and photobiology·2026
Same journal

Artemisitene formation during UVA-assisted Fenton oxidation of arteannuin B.

Photochemistry and photobiology·2026
Same journal

Surface alteration of Candida albicans after antifungal photodynamic therapy: A Raman spectroscopic study.

Photochemistry and photobiology·2026
Same journal

Phototherapies mediated by metallic nanoparticles and near-infrared radiation in skin cancer: A systematic review.

Photochemistry and photobiology·2026
Same journal

The burning question: Does exposure to low dose and low irradiance ultraviolet radiation lead to cutaneous DNA damage in people with skin types I-III?

Photochemistry and photobiology·2026
See all related articles

Molecular oxygen quenches horseradish peroxidase fluorescence slowly. This suggests the enzyme's heme site is protected, potentially explaining room temperature phosphorescence in its solutions.

Area of Science:

  • Biochemistry
  • Photophysics
  • Enzymology

Background:

  • Protoporphyrin IX is a key heme precursor.
  • Horseradish peroxidase (HRP) is a widely studied enzyme.
  • Oxygen quenching of fluorescence is a common method to study molecular interactions.

Purpose of the Study:

  • To investigate the quenching of protoporphyrin IX-adduct fluorescence in HRP by molecular oxygen.
  • To determine the bimolecular quenching rate constant.
  • To understand the accessibility of the heme binding site to oxygen.

Main Methods:

  • Intensity-resolved fluorescence spectroscopy.
  • Time-resolved fluorescence spectroscopy.
  • Stern-Volmer analysis.

Related Experiment Videos

Main Results:

  • The bimolecular quenching rate constant was determined to be 2 x 10^8 M^-1 s^-1.
  • This rate constant is exceptionally low for protein systems.
  • The heme binding site of HRP appears relatively inaccessible to molecular oxygen.

Conclusions:

  • The low quenching rate suggests steric hindrance at the HRP heme site.
  • This inaccessibility may explain the observation of room temperature phosphorescence.
  • Enzymatically generated triplet states in HRP are protected from oxygen in aerated solutions.