Andersson K K, Babcock G T, Hooper A B
Dept. of Genetics and Cell Biol., Univ. of Minnesota, St. Paul 55108.
Biochem Biophys Res Commun. 1991 Jan 15;174(1):358-63. doi: 10.1016/0006-291x(91)90528-f.
P460, an iron-containing chromophore at the active site of Hydroxylamine Oxidoreductase of the ammonia-oxidizing bacterium Nitrosomonas europaea, is a macrocycle of unknown structure with a Soret-like 460-nm absorption band in the ferrous form. The pigment can also be isolated in a peptide, "P460-Fragment". Resonance Raman spectroscopy (lambda ex = 457.9 nm) suggests that P460 is a new type of heme with symmetry properties lower than those of protophorphyrin IX or chlorins and similar to those of chlorophylls and isobacteriochlorins. Some of the resonance Raman vibrations of P460 are shifted in HAO as compared to those of P460-Fragment.
P460是氨氧化细菌欧洲亚硝化单胞菌（Nitrosomonas europaea）的羟胺氧化还原酶活性位点处的一种含铁发色团，它是一种结构未知的大环化合物，亚铁形式具有类似索雷特带的460纳米吸收带。该色素也可以以一种肽“P460片段”的形式分离出来。共振拉曼光谱（激发波长λ = 457.9纳米）表明，P460是一种新型血红素，其对称性低于原卟啉IX或二氢卟吩，与叶绿素和异细菌叶绿素相似。与P460片段相比，P460的一些共振拉曼振动在羟胺氧化还原酶中发生了位移。
