Nitrobacter winogradskyi cytochrome

The amino acid sequence of Nitrobacter winogradskyi cytochrome c [cytochrome c-550(s)] is more similar to those of human and horse cytochromes c than that of Nitrosomonas europaea cytochrome c (cytochrome c-552) (Table 3.4). Namely, N. winogradskyi seems to have appeared on Earth evolutionarily later than N. europaea, on the basis of the amino acid sequence of cytochrome c (Yamanaka and Fukumori, 1988). So it is expected that Earth might have been polluted by nitrous acid or nitrite in the period between the appearance of N. europaea and N. 

Fukuoka, M., Y. Fukumori, and T. Yamanaka. 1987. Nitrobacter winogradskyi cytochrome a C is an iron-sulfur molybdoenzyme having hemes a and c. J. Biochem. (Tokyo) 102 525-530. 

Fig. 3.5. The electron transfer pathways proposed for the oxidation of nitrite by Nitrobacter winogradskyi (prepared mainly on the basis of Aleem et al., 1963, 1965 Yamanaka et al., 1981a Tanaka et al., 1983 Nomoto et al., 1993). Dashes with arrows, unverified Cyt, cytochrome Pi, phosphate...

Nomoto T, Fukumori Y, Yamanaka T (1993) Membrane-bound cytochrome c is an alternative electron donor for cytochrome aa3 in Nitrobacter winogradskyi. J Bacteriol 175 4400-4404... 

Wehrfritz J-M, Carter JP, Soiro S, Richardson DJ (1997) Hydroxylamine oxidation in heterotro-phic nitrate-reducing soil bacteria and purification of hydroxylamine cytochrome c oxidore-ductase from Pseudomonas species. Arch Microbiol 166 421 —424 Wehrfritz J-M, Reilly A, Spiro S, Richardson DJ (1993) Purification of hydroxylamine oxidase from Thiosphaera pantotropha. Identification of electron acceptors that couple heterotrophic nitrification to aerobic denitrification. FEBS Lett 335 246-250 Wetzstein H-G, Ferguson SJ (1985) Respiration-dependent proton translocation and the mechanism of proton motive force generation in Nitrobacter winogradskyi. FEMS Microbiol Lett 30 87-92... 

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