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Structure and sequence of the multihaem cytochrome c3
Nature
|December 20, 1979
Summary
The molecular structure of cytochrome c3 from Desulfovibrio desulfuricans was determined using X-ray crystallography. This reveals a compact core of four exposed hemes, characteristic of this protein group.
Area of Science:
- Biochemistry
- Structural Biology
- Microbiology
Background:
- Cytochrome c3 is a key electron carrier in sulfate-reducing bacteria.
- Understanding its structure is crucial for elucidating electron transfer mechanisms.
Purpose of the Study:
- To determine the high-resolution molecular structure of cytochrome c3 from Desulfovibrio desulfuricans.
- To characterize the arrangement and accessibility of its heme groups.
Main Methods:
- X-ray crystallography at 2.5 A resolution.
- Amino acid sequence determination and alignment.
Main Results:
- The molecular structure was solved, revealing a single polypeptide chain.
- A compact core of four non-parallel hemes with significant solvent exposure was identified.
- The determined structure is consistent with other cytochrome c3 sequences.
Conclusions:
- The solved structure provides detailed insights into cytochrome c3's architecture.
- The heme exposure suggests a role in facilitating electron transfer.
- This structure is representative of the broader cytochrome c3 family.