P460 of hydroxylamine oxidoreductase of Nitrosomonas europaea: Soret resonance Raman evidence for a novel heme-like structure.
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.
Andersson
K K
KK
Dept. of Genetics and Cell Biol., Univ. of Minnesota, St. Paul 55108.
Babcock
G T
GT
Hooper
A B
AB
D001665:Binding Sites; D002734:Chlorophyll / Q000737:chemistry; D006418:Heme / Q000737:chemistry*; D009606:Nitrosomonas / Q000201:enzymology*; D010088:Oxidoreductases / Q000737:chemistry*; D010860:Pigments, Biological / Q000737:chemistry*; D011166:Porphyrins / Q000737:chemistry; D011487:Protein Conformation; D011524:Protoporphyrins / Q000737:chemistry; D013059:Spectrum Analysis, Raman
D010860:Pigments, Biological; D011166:Porphyrins; D011524:Protoporphyrins; D002734:Chlorophyll; C006969:chlorin; D006418:Heme; C028025:protoporphyrin IX; D010088:Oxidoreductases; C021401:hydroxylamine dehydrogenase