We have determined the 1.8 Å X-ray crystal structure of a monoheme c-type cytochrome,
cytochrome P460, from Nitrosomonas europea. The chromophore possesses unusual …

Cytochrome P460 and hydroxylamine oxidoreductase (HAO) of Nitrosomonas europaea
catalyze the oxidation of hydroxylamine. Cytochrome P460 contains an unidentified heme …

The enzymes hydroxylamine oxidoreductase and cytochrome (cyt) P460 contain related
unconventional “heme P460” cofactors. These cofactors are unusual in their inclusion of …

Abstract Cytochrome c554 (cyt c554), a tetra-heme cytochrome from Nitrosomonas
europaea, is an essential component in the biological nitrification pathway. In N. europaea …

The heme of cytochrome P460 of Nitrosomonas europaea, which is covalently crosslinked to
two cysteines of the polypeptide as with all c‐type cytochromes, has an additional novel …

The photosynthetic bacterium Rhodobacter sphaeroides produces a heme protein (SHP),
which is an unusual c-type cytochrome capable of transiently binding oxygen during …

The amino acid sequence of an oxygen-binding heme protein (SHP) from Rhodobacter
sphaeroides has been determined. The cysteines, which bind the single heme group in the …

The tetraheme cytochrome c554 (cyt c554) from Nitrosomonas europaea is an essential
electron transfer component in the biological oxidation of ammonia. The protein contains …

Abstract Cytochrome c 554 (cyt c 554) is a tetra-heme cytochrome involved in the oxidation
of NH 3 by Nitrosomonas europaea. The X-ray crystal structures of both the oxidized and …

The three‐dimensional structures of the native cytochrome c2 from Rhodopseudomonas
palustris and of its ammonia complex have been obtained at pH 4.4 and pH 8.5 …