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

Complex formation between ferredoxin and Synechococcus ferredoxin: nitrate oxidoreductase.

Masakazu Hirasawa1, Luis M Rubio, Jeannie L Griffin

  • 1Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA.

Biochimica Et Biophysica Acta
|February 12, 2004
PubMed
Summary

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

Photosynthesis regulation impacts carbon and nitrogen assimilation in the diazotrophic cyanobacterium Anabaena sp. PCC 7120.

The New phytologist·2026
Same author

Evolution of multicellularity genes in Cyanobacteria in the lead up to the great oxidation event.

Communications biology·2025
Same author

Retention of a SulP-family bicarbonate transporter in a periplasmic N2-fixing cyanobacterial endosymbiont of an open ocean diatom.

The ISME journal·2025
Same author

Intercellular communication in the fern endosymbiotic cyanobacterium <i>Nostoc azollae</i>.

mBio·2025
Same author

Distinct cell division features in <i>Anabaena</i>, a multicellular cyanobacterium.

Journal of bacteriology·2025
Same author

The role of the LysR-type transcription factor PacR in regulating nitrogen metabolism in Anabaena sp. PCC7120.

Physiologia plantarum·2025

Cyanobacterial nitrate reductase forms a high-affinity complex with ferredoxin, crucial for nitrate reduction. This electrostatic interaction, involving specific amino acids, is vital for enzyme function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Nitrate reductase is essential for nitrogen assimilation in cyanobacteria.
  • Ferredoxin serves as the physiological electron donor for this enzyme.

Purpose of the Study:

  • To investigate the role of ionic strength and electrostatic interactions in the ferredoxin-nitrate reductase complex formation.
  • To identify the amino acid residues involved in the ferredoxin-binding site of Synechococcus nitrate reductase.

Main Methods:

  • Spectroscopic analysis (absorbance and circular dichroism) to detect complex formation.
  • Enzyme activity assays using ferredoxin and methyl viologen as electron donors.
  • Chemical modification of Synechococcus nitrate reductase with arginine and lysine modifying reagents.

Related Experiment Videos

  • Site-specific mutagenesis of Anabaena ferredoxin variants.
  • Main Results:

    • High-affinity complex formation between Synechococcus nitrate reductase and ferredoxin is dependent on low ionic strength.
    • Enzyme activity with ferredoxin decreases at high ionic strength, while activity with methyl viologen remains unaffected.
    • Arginine and lysine residues on nitrate reductase, and negatively charged residues on ferredoxin, are critical for the electrostatic interaction and enzyme function.
    • Complex formation protects the enzyme's ferredoxin-dependent activity from chemical modification.

    Conclusions:

    • An electrostatically stabilized complex between ferredoxin and Synechococcus nitrate reductase is essential for efficient nitrate reduction.
    • Specific lysine and arginine residues on the reductase and charged residues on ferredoxin mediate this interaction.
    • Understanding these interactions provides insight into the regulation of nitrogen metabolism in cyanobacteria.