Pseudomonas cytochrome c551 at 2.0 A resolution: enlargement of the cytochrome c family. | Zendy

Robert J. Almassy | Zendy; Richard E. Dickerson | Zendy

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Pseudomonas cytochrome c551 at 2.0 A resolution: enlargement of the cytochrome c family.

Author(s) -

Robert J. Almassy,

Richard E. Dickerson

Publication year - 1978

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.75.6.2674

Subject(s) - cytochrome , heme , biochemistry , electron transport chain , cytochrome c , hemeprotein , cytochrome b , biology , photosynthesis , pseudomonas , chemistry , bacteria , gene , enzyme , mitochondrion , genetics , mitochondrial dna

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.

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