1AS7
STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE
Summary for 1AS7
| Entry DOI | 10.2210/pdb1as7/pdb |
| Descriptor | NITRITE REDUCTASE, COPPER (II) ION (3 entities in total) |
| Functional Keywords | oxidoreductase, nitrite, copper, denitrification |
| Biological source | Alcaligenes faecalis |
| Cellular location | Periplasm: P38501 |
| Total number of polymer chains | 3 |
| Total formula weight | 111572.94 |
| Authors | Murphy, M.E.P.,Adman, E.T.,Turley, S. (deposition date: 1997-08-13, release date: 1998-02-25, Last modification date: 2024-05-22) |
| Primary citation | Murphy, M.E.,Turley, S.,Adman, E.T. Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications. J.Biol.Chem., 272:28455-28460, 1997 Cited by PubMed Abstract: The structures of oxidized, reduced, nitrite-soaked oxidized and nitrite-soaked reduced nitrite reductase from Alcaligenes faecalis have been determined at 1.8-2.0 A resolution using data collected at -160 degrees C. The active site at cryogenic temperature, as at room temperature, contains a tetrahedral type II copper site liganded by three histidines and a water molecule. The solvent site is empty when crystals are reduced with ascorbate. A fully occupied oxygen-coordinate nitrite occupies the solvent site in crystals soaked in nitrite. Ascorbate-reduced crystals soaked in a glycerol-methanol solution and nitrite at -40 degrees C remain colorless at -160 degrees C but turn amber-brown when warmed, suggesting that NO is released. Nitrite is found at one-half occupancy. Five new solvent sites in the oxidized nitrite bound form exhibit defined but different occupancies in the other three forms. These results support a previously proposed mechanism by which nitrite is bound primarily by a single oxygen atom that is protonable, and after reduction and cleavage of that N-O bond, NO is released leaving the oxygen atom bound to the Cu site as hydroxide or water. PubMed: 9353305DOI: 10.1074/jbc.272.45.28455 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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