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1AS7

STRUCTURE OF ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE

Summary for 1AS7
Entry DOI10.2210/pdb1as7/pdb
DescriptorNITRITE REDUCTASE, COPPER (II) ION (3 entities in total)
Functional Keywordsoxidoreductase, nitrite, copper, denitrification
Biological sourceAlcaligenes faecalis
Cellular locationPeriplasm: P38501
Total number of polymer chains3
Total formula weight111572.94
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 citationMurphy, 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: 9353305
DOI: 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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数据于2025-07-23公开中

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