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

Nitrate binding to Limulus polyphemus subunit type II hemocyanin and its functional implications

B Hazes1, K A Magnus, K H Kalk

  • 1Department of Chemical Physics, University of Groningen, AG, The Netherlands.

Journal of Molecular Biology
|October 4, 1996
PubMed
Summary

Horseshoe crab hemocyanin

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

Allosteric modulation of Callinectes sapidus hemocyanin by binding of L-lactate.

Biochemistry·2015
Same author

Comparison of the physical and functional properties of the 48-subunit native molecule and the 24- and 12-subunit dissociation intermediates of Limulus polyphemus hemocyanin.

Biochemistry·2015
Same author

The dead-end elimination theorem and its use in protein side-chain positioning.

Nature·2011
Same author

Assembly processes in oligomers containing structurally distinct subunits: respiratory proteins as models.

Biophysical journal·2009
Same author

New insights into the proton-dependent oxygen affinity of Root effect haemoglobins.

Acta physiologica Scandinavica·2004
Same author

Probing the limits of the molecular replacement method: the case of Trypanosoma brucei phosphoglycerate kinase.

Acta crystallographica. Section D, Biological crystallography·2004

Area of Science:

  • Biochemistry
  • Structural Biology
  • Zoology

Background:

  • Horseshoe crab hemocyanin (hemolymph oxygen carrier) exhibits cooperative oxygen binding.
  • It is allosterically regulated by protons, chloride ions, and divalent cations.

Purpose of the Study:

  • To determine the crystal structure of Limulus polyphemus subunit type II hemocyanin.
  • To investigate the binding of nitrate ions and their effect on oxygen affinity.

Main Methods:

  • X-ray crystallography to determine protein structure.
  • Oxygen-binding assays to measure hemocyanin affinity.

Main Results:

  • Crystal structure revealed a nitrate ion bound at the interface of the first and second domains.

Related Experiment Videos

  • The nitrate-binding site overlaps with the allosteric chloride-binding site.
  • Nitrate binding, similar to chloride, reduces hemocyanin oxygen affinity.

    • Conclusions:

    • The overlapping binding sites suggest other anions, like bicarbonate, may also act as allosteric effectors.
    • Bicarbonate could potentially lower hemocyanin oxygen affinity, impacting respiration.
    • Further research is needed to understand the complex physiological interplay of these effectors.