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

Oxidation state-dependent conformational changes in cytochrome c.

A M Berghuis1, G D Brayer

  • 1Department of Biochemistry, University of British Columbia, Vancouver, Canada.

Journal of Molecular Biology
|February 20, 1992
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

Structural studies of the final enzyme in the alpha-aminoadipate pathway-saccharopine dehydrogenase from Saccharomyces cerevisiae.

Journal of molecular biology·2007
Same author

Comparative analysis of folding and substrate binding sites between regulated hexameric type II citrate synthases and unregulated dimeric type I enzymes.

Biochemistry·2001
Same author

Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase.

Biochemistry·2001
Same author

Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase.

Biochemistry·2001
Same author

Crystallization and preliminary X-ray diffraction studies of glycerol 3-phosphate cytidylyltransferase from Staphylococcus aureus.

Acta crystallographica. Section D, Biological crystallography·2001
Same author

Crystal structure of the lytic transglycosylase from bacteriophage lambda in complex with hexa-N-acetylchitohexaose.

Biochemistry·2001

Structural analysis of yeast iso-1-cytochrome c reveals subtle conformational changes between oxidation states, primarily involving heme adjustments and water molecule movement, not significant shifts in the polypeptide chain.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • Yeast iso-1-cytochrome c is a crucial protein in cellular respiration.
  • Understanding its structural dynamics across oxidation states is key to elucidating electron transfer mechanisms.

Purpose of the Study:

  • To perform high-resolution 3D structural analysis of yeast iso-1-cytochrome c in both oxidized and reduced states.
  • To compare these structures and identify subtle conformational changes related to oxidation state.

Main Methods:

  • Isomorphous crystalline material was used for structure determination.
  • High-resolution three-dimensional structural analyses were performed for both oxidation states.

Main Results:

Related Experiment Videos

  • Oxidation state-dependent changes are mainly adjustments in heme structure, internal water molecule positions, and polypeptide chain thermal parameters.
  • Minimal explicit polypeptide chain positional shifts were observed, with retained main-chain hydrogen bonds.
  • Specific residues (37-39, 47-59, 65-72, 81-85) showed altered mobility, particularly Asn52, Tyr67, and Phe82.
  • Internal water molecule Wat166 plays a significant role in stabilizing heme iron through interactions and hydrogen bonding network alterations.

    • Conclusions:

    • Conformational changes in yeast iso-1-cytochrome c are subtle and localized, primarily affecting heme environment and water molecule interactions.
    • The internal water molecule Wat166 is critical for stabilizing both heme oxidation states.
    • Structural changes are focused around the heme propionate group, Wat166, and the Met80 ligand, linked by intermediary interactions.