Purification of cytochrome a 1 c 1 from Nitrobacter agilis and characterization of nitrite oxidation system of the bacterium

@article{Tanaka2004PurificationOC,
  title={Purification of cytochrome a 1 c 1 from Nitrobacter agilis and characterization of nitrite oxidation system of the bacterium},
  author={Yoshikazu Tanaka and Yoshihiro Fukumori and Tateo Yamanaka},
  journal={Archives of Microbiology},
  year={2004},
  volume={135},
  pages={265-271}
}
Cytochrome a 1 c 1 was highly purified from Nitrobacter agilis. The cytochrome contained heme a and heme c of equimolar amount, and its reduced form showed absorption peaks at 587, 550, 521, 434 and 416 nm. Molecular weight per heme a of the cytochrome was estimated to be approx. 100,000–130,000 from the amino acid composition. A similar value was obtained by determining the protein content per heme a. The cytochrome molecule was composed of three subunits with molecular weights of 55,000, 29… CONTINUE READING

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