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Studies on cytochrome c oxidase, IV[1--3]. Primary structure and function of subunit II
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
|April 1, 1979
Summary
Beef heart cytochrome c oxidase subunit II shares sequence homologies with blue copper proteins. This suggests it belongs to the same protein family and possesses a type I copper binding site.
Area of Science:
- Biochemistry
- Protein Science
- Molecular Biology
Background:
- Cytochrome c oxidase is a crucial enzyme in cellular respiration.
- Blue copper proteins are involved in electron transfer processes.
- Understanding subunit II's structure provides insights into enzyme function.
Purpose of the Study:
- To determine the amino acid sequence of beef heart cytochrome c oxidase polypeptide II.
- To compare this sequence with known blue copper proteins.
- To identify potential functional and structural relationships.
Main Methods:
- Amino acid sequencing of polypeptide II.
- Comparative sequence analysis.
- Bioinformatic comparisons with azurins, plastocyanins, and stellacyanins.
Main Results:
- The primary structure of beef heart cytochrome c oxidase subunit II was elucidated.
- Significant sequence homologies were found between subunit II and blue copper proteins.
- These homologies suggest subunit II is a member of the blue copper protein family.
Conclusions:
- Beef heart cytochrome c oxidase subunit II exhibits characteristics of a blue copper protein.
- The sequence homology points to a conserved copper binding site involving histidines and sulfur-containing amino acids.
- This finding deepens the understanding of electron transfer mechanisms in cytochrome c oxidase.