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

The relationship between structure and function for the sulfite reductases

B R Crane1, E D Getzoff

  • 1Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA. crane@scripps.edu

Current Opinion in Structural Biology
|December 1, 1996
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

The structural biochemistry of the superoxide dismutases.

Biochimica et biophysica acta·2009
Same author

Site-specific mutations provide new insights into the origin of pH effects and alternative spectral forms in the photoactive yellow protein from Halorhodospira halophila.

Biochemistry·2003
Same author

Electron tunneling in single crystals of Pseudomonas aeruginosa azurins.

Journal of the American Chemical Society·2001
Same author

Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457.

Biochemistry·2001
Same author

Probing the open state of cytochrome P450cam with ruthenium-linker substrates.

Proceedings of the National Academy of Sciences of the United States of America·2001
Same author

Properties of photogenerated tryptophan and tyrosyl radicals in structurally characterized proteins containing rhenium(I) tricarbonyl diimines.

Journal of the American Chemical Society·2001
Same journal

Tomogram exploration through template matching and deep learning.

Current opinion in structural biology·2026
Same journal

A comparative review of cryo-electron ptychography: Biological applications and future perspectives.

Current opinion in structural biology·2026
Same journal

Metabolic disruptions through a three-dimensional genomic lens.

Current opinion in structural biology·2026
Same journal

Collective variable design for biomolecular conformational dynamics.

Current opinion in structural biology·2026
Same journal

Polymer scaling in protein crowding: From dilute coils to semidilute meshes.

Current opinion in structural biology·2026
Same journal

Tuning the physicochemical properties of rationally designed protein-based biomolecular condensates.

Current opinion in structural biology·2026
See all related articles

Sulfite and nitrite reductases, essential enzymes for life, feature a unique siroheme and Fe4S4 cluster. The Escherichia coli sulfite reductase structure reveals key catalytic features and a common enzyme family unit.

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Sulfite and nitrite reductases catalyze essential six-electron reductions vital for life.
  • These enzymes share a unique prosthetic group: siroheme covalently linked to an iron-sulfur cluster (Fe4S4).

Purpose of the Study:

  • To elucidate the structural basis of catalytic mechanisms in sulfite and nitrite reductases.
  • To understand the conserved structural features within this enzyme family.

Main Methods:

  • X-ray crystallography of the sulfite reductase hemoprotein from Escherichia coli.
  • Integration with existing biochemical and spectroscopic data.

Main Results:

  • The crystallographic structure reveals key structural determinants for enzymatic catalysis.

Related Experiment Videos

  • Identified a common symmetric structural motif shared across diverse sulfite and nitrite reductases.

    • Conclusions:

    • The determined structure provides critical insights into the catalytic mechanisms of these vital enzymes.
    • Highlights a conserved structural unit suggesting evolutionary links within the reductase family.