1as8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
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 .. | 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. | ||
==About this Structure== | ==About this Structure== | ||
1AS8 is a | 1AS8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with CU and NO2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_1.7.2.1 Transferred entry: 1.7.2.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.99.3 1.7.99.3] Structure known Active Sites: CU1, CU2, CU3, CU4, CU5 and CU6. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AS8 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:27:42 2007'' | ||
Revision as of 13:22, 5 November 2007
|
STRUCTURE OF NITRITE BOUND TO REDUCED ALCALIGENES FAECALIS NITRITE REDUCTASE AT CRYO TEMPERATURE
OverviewOverview
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.
About this StructureAbout this Structure
1AS8 is a Single protein structure of sequence from Alcaligenes faecalis with CU and NO2 as ligands. Active as Transferred entry: 1.7.2.1, with EC number 1.7.99.3 Structure known Active Sites: CU1, CU2, CU3, CU4, CU5 and CU6. Full crystallographic information is available from OCA.
ReferenceReference
Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications., Murphy ME, Turley S, Adman ET, J Biol Chem. 1997 Nov 7;272(45):28455-60. PMID:9353305
Page seeded by OCA on Mon Nov 5 12:27:42 2007