The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase.
Here we investigate the structure of the two types of copper site in nitrite reductase from Alcaligenes xylosoxidans, the molecular organisation of the enzyme when the type-2 copper is absent, and its mode of substrate binding. X-ray absorption studies provide evidence for a fourth ligand at the type-2 Cu, that substrate binds to this site and indicates that this binding does not change the type-1 Cu centre. The substrate replaces a putative water ligand and is accommodated by a lengthening of the Cu-histidine bond by approximately 0.08 A. Modelling suggests a similarity between this unusual type-2 Cu site and the Zn site in carbonic anhydrase and that nitrite is anchored by hydrogen bonds to an unligated histidine present in the type-2 Cu cavity.
Strange
R W
RW
Molecular Biophysics Group, Daresbury Laboratory, Warrington, Cheshire, UK.
Dodd
F E
FE
Abraham
Z H
ZH
Grossmann
J G
JG
Brüser
T
T
Eady
R R
RR
Smith
B E
BE
Hasnain
S S
SS
D015502:Absorptiometry, Photon; D000421:Alcaligenes / Q000201:enzymology; D001665:Binding Sites; D002256:Carbonic Anhydrases / Q000737:chemistry* / Q000378:metabolism*; D003300:Copper / Q000378:metabolism*; D008958:Models, Molecular; D009572:Nitrite Reductases / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D013482:Superoxide Dismutase / Q000737:chemistry / Q000378:metabolism; D015032:Zinc / Q000378:metabolism*
D003300:Copper; D013482:Superoxide Dismutase; D009572:Nitrite Reductases; D002256:Carbonic Anhydrases; D015032:Zinc