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Science (New York, N.Y.)1992; 258(5089); 1748-1755; doi: 10.1126/science.1334573

Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c.

Abstract: The crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c was determined at 2.3 A resolution. This structure reveals a possible electron transfer pathway unlike any previously proposed for this extensively studied redox pair. The shortest straight line between the two hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193, Gly192, and finally Trp191, the indole ring of which is perpendicular to, and in van der Waals contact with, the peroxidase heme. The crystal structure at 2.8 A of a complex between yeast cytochrome c peroxidase and horse heart cytochrome c was also determined. Although crystals of the two complexes (one with cytochrome c from yeast and the other with cytochrome c from horse) grew under very different conditions and belong to different space groups, the two complex structures are closely similar, suggesting that cytochrome c interacts with its redox partners in a highly specific manner.
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Publication Date: 1992-12-11 PubMed ID: 1334573DOI: 10.1126/science.1334573Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • Non-P.H.S.
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research focuses on the understanding of the electron transfer mechanism in yeast, specifically between cytochrome c peroxidase and cytochrome c, by means of analyzing their crystal structures at a 2.3 A resolution. The paper reveals an unprecedented pathway for this transfer, terminating at Trp191. Similar observations were also conducted for the horse heart cytochrome c.

Overview of the Research

  • The researchers present an in-depth analysis of the crystal structure of a 1:1 complex between yeast cytochrome c peroxidase and yeast iso-1-cytochrome c. The crystal structure was determined at a resolution of 2.3 A.
  • From this analysis, they identify a possible route for electron transfer. This route is unlike any proposed previously for this redox pair, which has been extensively studied.

Electron Transfer Pathway

  • In this newly discovered electron transfer pathway, the shortest straight line between the two hemes closely follows the peroxidase backbone chain of residues Ala194, Ala193, Gly192, and finally Trp191.
  • Trp191’s indole ring is positioned perpendicular to and in van der Waals contact with the peroxidase heme, indicating the site of electron transfer.

Comparative Study with Horse Heart Cytochrome c

  • The researchers also examined the crystal structure of a complex between yeast cytochrome c peroxidase and horse heart cytochrome c at a resolution of 2.8 A.
  • Although the conditions under which the crystals for these two complexes (one with cytochrome c from yeast, the other with cytochrome c from a horse) were grown differed substantially and belonged to differing space groups, the structures of the two complexes were found to be very similar.
  • This suggests that cytochrome c interacts with its redox partners in a highly specific manner, irrespective of the source of cytochrome c.

Conclusion

  • In summary, the research provides new insights into the mechanism of electron transfer between cytochrome c peroxidase and cytochrome c, a significant process in energy production. The findings indicate a unique pathway for electron transfer and highlight the specificity of interaction between cytochrome c and its redox partners.

Cite This Article

APA
Pelletier H, Kraut J. (1992). Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science, 258(5089), 1748-1755. https://doi.org/10.1126/science.1334573

Publication

Science (New York, N.Y.)
ISSN: 0036-8075
NlmUniqueID: 0404511
Country: United States
Language: English
Volume: 258
Issue: 5089
Pages: 1748-1755

Researcher Affiliations

Pelletier, H
  • Department of Chemistry, University of California, San Diego, La Jolla 92093-0317.
Kraut, J

    MeSH Terms

    • Amino Acid Sequence
    • Animals
    • Binding Sites
    • Cytochrome c Group / chemistry
    • Cytochrome c Group / metabolism
    • Cytochrome-c Peroxidase / chemistry
    • Cytochrome-c Peroxidase / metabolism
    • Electron Transport
    • Heme / metabolism
    • Horses
    • Models, Molecular
    • Molecular Sequence Data
    • Protein Conformation
    • Saccharomyces cerevisiae / metabolism
    • X-Ray Diffraction / methods

    Grant Funding

    • DK07233 / NIDDK NIH HHS

    Citations

    This article has been cited 131 times.
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