| Literature DB >> 96440 |
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.Entities:
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Year: 1978 PMID: 96440 PMCID: PMC392625 DOI: 10.1073/pnas.75.6.2674
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205