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A di-heme cytochrome c peroxidase from Nitrosomonas europaea catalytically active in both the oxidized and half-reduced states
1994
Journal of Biological Chemistry
A di-c-heme containing cytochrome (cytochrome c553 peroxidase) has been isolated from the chemoautotrophic bacterium Nitrosomonas europaea. Sequence analysis of the N terminus and the two heme-containing peptides generated by digestion of the enzyme with trypsin show 40% homology overall to sequences reported for the di-heme peroxidase from Pseudomonas aeruginosa (Rönnberg, M., Kalkkinen, N., and Ellfolk, N. (1989) FEBS Lett. 250, 175-178). At room temperature and pH 7.0, one heme is low spin
pmid:8163487
fatcat:mvi6a6vwcfgxpf7v2e6jwwlexa