Purification, primary structure, and evolution of cytochrome c-550 from the magnetic bacterium, Magnetospirillum magnetotacticum.
Cytochrome c-550 was purified from Magnetospirillum magnetotacticum to an electrophoretically homogeneous state, and some of its properties were determined. The cytochrome showed absorption peaks at 528 and 409 nm in the oxidized form, and at 550, 521, and 414 nm in the reduced form. Its midpoint redox potential at pH 7.0 was determined to be +289 mV. The primary structure of cytochrome c-550 was determined. Cytochrome c is composed of 97 amino acid residues, and its molecular weight was calculated to be 10,873, including heme c. Its primary structure is very similar to those of Rhodospirillum fulvum and Rhodospirillum molischianum cytochromes c2, suggesting that M. magnetotacticum is phylogenetically related to photosynthetic bacteria.
Yoshimatsu
K
K
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
Fujiwara
T
T
Fukumori
Y
Y
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D003574:Cytochrome c Group / Q000737:chemistry* / Q000302:isolation & purification; D006090:Gram-Negative Bacteria / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments; D010802:Phylogeny; D016415:Sequence Alignment; D017421:Sequence Analysis
D000596:Amino Acids; D003574:Cytochrome c Group; D010446:Peptide Fragments; C031732:cytochrome C-550