Abstract
The structure of respiratory cytochrome c551 of Pseudomonas aeruginosa, with 82 amino acids, has been solved by x-ray analysis and refined to a crystallographic R factor of 16.2%. It has the same basic folding pattern and hydrophobic heme environment as cytochromes c, c2, and c550, except for a large deletion at the bottom of the heme crevice. This same "cytochrome fold" appears to be present in photosynthetic cytochromes c of green and purple sulfur bacteria, and algal cytochromes f, suggesting a common evolutionary origin for electron transport chains in photosynthesis and respiration.
MeSH Terms
Bacterial Proteins
Biological Evolution
Cytochrome c Group
Cytochromes
Heme
Models, Molecular
Protein Conformation
Pseudomonas aeruginosa/enzymology
X-Ray Diffraction
Chemicals
Bacterial Proteins
Cytochrome c Group
Cytochromes
Heme
cytochrome C(551)
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Almassy R J
Dickerson R E
References (12)
12 references, click to expand
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