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

Bacterial ferritin contains 24 haem groups.

F H Kadir1, G R Moore

  • 1Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, UK.

FEBS Letters
|October 1, 1990
PubMed
Summary

Researchers studied Pseudomonas aeruginosa bacterioferritin, a protein involved in iron storage. They found that the protein

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 blood picture in cases of retained fetal membranes in cattle.

Journal of the American Veterinary Medical Association·2010
Same author

Effects of stilbestrol in retained placenta.

Journal of the American Veterinary Medical Association·2010
Same author

Effects of stilbestrol on pyometra following retained fetal membranes.

Journal of the American Veterinary Medical Association·2010
Same author

Effects of chorionic gonadotropin on cystic ovaries in the cow.

Veterinary medicine·2010
Same author

Heredity as a guide in dentofacial orthopedics.

American journal of orthodontics and oral surgery·2010
Same author

The causes and diagnosis of infertility in bulls.

Journal of the American Veterinary Medical Association·2010

Area of Science:

  • Biochemistry
  • Microbiology
  • Protein Chemistry

Background:

  • Pseudomonas aeruginosa bacterioferritin (also known as cytochrome b1 or cytochrome b557) is a key iron-storage protein.
  • Understanding its heme binding is crucial for elucidating its biological function.

Purpose of the Study:

  • To characterize the heme loading and removal dynamics of Pseudomonas aeruginosa bacterioferritin.
  • To investigate the role of the protein core in heme incorporation.

Main Methods:

  • Isolation of Pseudomonas aeruginosa bacterioferritin with varying heme content.
  • Preparation of completely heme-free and fully heme-loaded protein variants.
  • Spectrophotometric analysis to determine heme loading.

Main Results:

  • The protein was isolated with 9 hemes per 24 subunits.
  • Completely heme-free and fully heme-loaded (24 hemes per 24 subunits) forms were successfully prepared.
  • The protein core minimally impacts heme addition or removal.
  • An absorbance ratio (278 nm:417 nm, oxidized) can quantify heme loading in the non-heme-iron-loaded protein.

Conclusions:

  • Heme loading and removal in Pseudomonas aeruginosa bacterioferritin are not significantly hindered by the protein core.
  • A spectrophotometric method is proposed for estimating heme loading levels.

Related Experiment Videos