2e81: Difference between revisions
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|PDB= 2e81 |SIZE=350|CAPTION= <scene name='initialview01'>2e81</scene>, resolution 2.0Å | |PDB= 2e81 |SIZE=350|CAPTION= <scene name='initialview01'>2e81</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HOA:HYDROXYAMINE'>HOA</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Nitrite_reductase_(cytochrome;_ammonia-forming) Nitrite reductase (cytochrome; ammonia-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.2 1.7.2.2] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrite_reductase_(cytochrome;_ammonia-forming) Nitrite reductase (cytochrome; ammonia-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.2 1.7.2.2] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1fs7|1FS7]], [[1fs8|1FS8]], [[1fs9|1FS9]], [[2e80|2E80]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e81 OCA], [http://www.ebi.ac.uk/pdbsum/2e81 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e81 RCSB]</span> | |||
}} | }} | ||
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[[Category: Einsle, O.]] | [[Category: Einsle, O.]] | ||
[[Category: Kroneck, P M.H.]] | [[Category: Kroneck, P M.H.]] | ||
[[Category: multiheme cytochrome]] | [[Category: multiheme cytochrome]] | ||
[[Category: nitrite reductase]] | [[Category: nitrite reductase]] | ||
[[Category: reaction intermediate]] | [[Category: reaction intermediate]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:45:07 2008'' | ||
Revision as of 02:45, 31 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Nitrite reductase (cytochrome; ammonia-forming), with EC number 1.7.2.2 | ||||||
| Related: | 1FS7, 1FS8, 1FS9, 2E80
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cytochrome c Nitrite Reductase from Wolinella succinogenes with bound intermediate hydroxylamine
OverviewOverview
Cytochrome c nitrite reductase catalyzes the six-electron reduction of nitrite to ammonia without the release of potential reaction intermediates, such as NO or hydroxylamine. On the basis of the crystallographic observation of reaction intermediates and of density functional calculations, we present a working hypothesis for the reaction mechanism of this multiheme enzyme which carries a novel lysine-coordinated heme group (Fe-Lys). It is proposed that nitrite reduction starts with a heterolytic cleavage of the N-O bond which is facilitated by a pronounced back-bonding interaction of nitrite coordinated through nitrogen to the reduced (Fe(II)) but not the oxidized (Fe(III)) active site iron. This step leads to the formation of an [FeNO](6) species and a water molecule and is further facilitated by a hydrogen bonding network that induces an electronic asymmetry in the nitrite molecule that weakens one N-O bond and strengthens the other. Subsequently, two rapid one-electron reductions lead to an [FeNO](8) form and, by protonation, to an Fe(II)-HNO adduct. Hereafter, hydroxylamine will be formed by a consecutive two-electron two-proton step which is dehydrated in the final two-electron reduction step to give ammonia and an additional water molecule. A single electron reduction of the active site closes the catalytic cycle.
About this StructureAbout this Structure
2E81 is a Single protein structure of sequence from Wolinella succinogenes. Full crystallographic information is available from OCA.
ReferenceReference
Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase., Einsle O, Messerschmidt A, Huber R, Kroneck PM, Neese F, J Am Chem Soc. 2002 Oct 2;124(39):11737-45. PMID:12296741
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