A copper-containing nitrite reductase from
Alcaligenes xylosoxidansNCIMB 11015 has its own unique blue or type 1 copper proteinresonance Raman spectrum in the usual Cu-S
Cys stretching region,
![](/images/gifchars/nu.gif)
(Cu-S
Cys), with a pair of strong peaks at 412
and 420 cm
-1 anda weak peak at 364 cm
-1. The predominantly
![](/images/gifchars/nu.gif)
(Cu-S
Cys) Ramanb
ands at 412, 420,
and 364 cm
-1 of the type 1 copper site allshifted to higher frequencies upon binding of nitrite to the type 2copper site,
and the resonance Raman difference spectra progressively intensified with the increments of nitrite ion concentration.Positive support for substrate binding to the type 2 copper isprovided by the
![](/images/gifchars/nu.gif)
(Cu-S
Cys) b
ands in the resonance Ramanspectrum of a type 2 copper-depleted enzyme, which is insensitiveto the presence of NO
2-. The shift to higher frequency of theRaman b
ands of the type 1 copper center with the addition ofnitrite ions suggests a stronger Cu-S
Cys interaction in the substrate-bound
A. xylosoxidans nitrite reductase.