2ppf

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[[Image:2ppf.jpg|left|200px]]
[[Image:2ppf.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 2ppf |SIZE=350|CAPTION= <scene name='initialview01'>2ppf</scene>, resolution 1.65&Aring;
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The line below this paragraph, containing "STRUCTURE_2ppf", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(NO-forming) Nitrite reductase (NO-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.1 1.7.2.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= nirK, nir ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=511 Alcaligenes faecalis])
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-->
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|DOMAIN=
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{{STRUCTURE_2ppf| PDB=2ppf | SCENE= }}
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|RELATEDENTRY=[[1j9r|1J9R]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ppf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ppf OCA], [http://www.ebi.ac.uk/pdbsum/2ppf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ppf RCSB]</span>
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}}
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'''Reduced mutant D98N of AfNiR exposed to nitric oxide'''
'''Reduced mutant D98N of AfNiR exposed to nitric oxide'''
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Stable copper-nitrosyl formation by nitrite reductase in either oxidation state., Tocheva EI, Rosell FI, Mauk AG, Murphy ME, Biochemistry. 2007 Oct 30;46(43):12366-74. Epub 2007 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17924665 17924665]
Stable copper-nitrosyl formation by nitrite reductase in either oxidation state., Tocheva EI, Rosell FI, Mauk AG, Murphy ME, Biochemistry. 2007 Oct 30;46(43):12366-74. Epub 2007 Oct 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17924665 17924665]
[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
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[[Category: Nitrite reductase (NO-forming)]]
 
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Murphy, M E.P.]]
[[Category: Murphy, M E.P.]]
[[Category: Tocheva, E I.]]
[[Category: Tocheva, E I.]]
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[[Category: bacteria]]
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[[Category: Bacteria]]
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[[Category: copper]]
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[[Category: Copper]]
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[[Category: d98n]]
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[[Category: D98n]]
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[[Category: denitrification]]
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[[Category: Denitrification]]
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[[Category: nitric oxide]]
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[[Category: Nitric oxide]]
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[[Category: nitrite reductase]]
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[[Category: Nitrite reductase]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:35:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:39:03 2008''
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Revision as of 10:35, 4 May 2008

Image:2ppf.jpg

Template:STRUCTURE 2ppf

Reduced mutant D98N of AfNiR exposed to nitric oxide


Overview

Nitrite reductase (NiR) is an enzyme that uses type 1 and type 2 copper sites to reduce nitrite to nitric oxide during bacterial denitrification. A copper-nitrosyl intermediate is a proposed, yet poorly characterized feature of the NiR catalytic cycle. This intermediate is formally described as Cu(I)-NO+ and is proposed to be formed at the type 2 copper site after nitrite binding and electron transfer from the type 1 copper site. In this study, copper-nitrosyl complexes were formed by prolonged exposure of exogenous NO to crystals of wild-type and two variant forms of NiR from Alcaligenes faecalis (AfNiR), and the structures were determined to 1.8 A or better resolution. Exposing oxidized wild-type crystals to NO results in the reverse reaction and formation of nitrite that remains bound at the active site. In a type 1 copper site mutant (H145A) that is incapable of electron transfer to the type 2 site, the reverse reaction is not observed. Instead, in both oxidized and reduced H145A crystals, NO is observed bound in a side-on manner to the type 2 copper. In AfNiR, Asp98 forms hydrogen bonds to both substrate and product bound to the type 2 Cu. In the D98N variant, NO is bound side-on but is more disordered when observed for the wild-type enzyme. The solution EPR spectra of the crystallographically characterized NiR-NO complexes indicate the presence of an oxidized type 2 copper site and thus are interpreted as resulting from stable copper-nitrosyls and formally assigned as Cu(II)-NO-. A reaction scheme in which a second NO molecule is oxidized to nitrite can account for the formation of a Cu(II)-NO- species after exposure of the oxidized H145A variant to NO gas.

About this Structure

2PPF is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.

Reference

Stable copper-nitrosyl formation by nitrite reductase in either oxidation state., Tocheva EI, Rosell FI, Mauk AG, Murphy ME, Biochemistry. 2007 Oct 30;46(43):12366-74. Epub 2007 Oct 9. PMID:17924665 Page seeded by OCA on Sun May 4 13:35:08 2008

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