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| | ==Kuenenia stuttgartiensis hydroxylamine oxidoreductase== | | ==Kuenenia stuttgartiensis hydroxylamine oxidoreductase== |
| - | <StructureSection load='4n4j' size='340' side='right' caption='[[4n4j]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4n4j' size='340' side='right'caption='[[4n4j]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n4j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"candidatus_kuenenia_stuttgartiensis"_schmid_et_al._2000 "candidatus kuenenia stuttgartiensis" schmid et al. 2000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N4J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n4j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Kuenenia_stuttgartiensis Candidatus Kuenenia stuttgartiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N4J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4J FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HG1:1-[(4-CYCLOHEXYLBUTANOYL)(2-HYDROXYETHYL)AMINO]-1-DEOXY-D-GLUCITOL'>HG1</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n4k|4n4k]], [[4n4l|4n4l]], [[4n4m|4n4m]], [[4n4n|4n4n]], [[4n4o|4n4o]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HG1:1-[(4-CYCLOHEXYLBUTANOYL)(2-HYDROXYETHYL)AMINO]-1-DEOXY-D-GLUCITOL'>HG1</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxylamine_dehydrogenase Hydroxylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.6 1.7.2.6] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4j OCA], [https://pdbe.org/4n4j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4j RCSB], [https://www.ebi.ac.uk/pdbsum/4n4j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4j ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n4j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n4j RCSB], [http://www.ebi.ac.uk/pdbsum/4n4j PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HAO_KUEST HAO_KUEST] Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor (PubMed:21964329, PubMed:24302732). Does not oxidize hydroxylamine to nitrite (PubMed:24302732). Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological (PubMed:21964329, PubMed:24302732).<ref>PMID:21964329</ref> <ref>PMID:24302732</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 4n4j" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Candidatus kuenenia stuttgartiensis schmid et al. 2000]] | + | [[Category: Candidatus Kuenenia stuttgartiensis]] |
| - | [[Category: Hydroxylamine dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Barends, T R.M B]] | + | [[Category: Barends TRMB]] |
| - | [[Category: Butt, J N]] | + | [[Category: Butt JN]] |
| - | [[Category: Dietl, A]] | + | [[Category: Dietl A]] |
| - | [[Category: Jetten, M S.M]] | + | [[Category: Jetten MSM]] |
| - | [[Category: Kartal, B]] | + | [[Category: Kartal B]] |
| - | [[Category: Keltjens, J T]] | + | [[Category: Keltjens JT]] |
| - | [[Category: Maalcke, W J]] | + | [[Category: Maalcke WJ]] |
| - | [[Category: Marritt, S J]] | + | [[Category: Marritt SJ]] |
| - | [[Category: C-type cytochrome]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
HAO_KUEST Catalyzes the oxidation of hydroxylamine to nitric oxide with cytochrome c acting as an electron acceptor (PubMed:21964329, PubMed:24302732). Does not oxidize hydroxylamine to nitrite (PubMed:24302732). Also able to catalyze the four-electron oxidation of hydrazine to N(2) in vitro with reduced efficiency; however, this reaction is probably not physiological (PubMed:21964329, PubMed:24302732).[1] [2]
Publication Abstract from PubMed
Nitric oxide (NO) is an important molecule in all domains of life with significant biological functions in both pro- and eukaryotes. Anaerobic ammonium-oxidizing (anammox) bacteria that contribute substantially to the release of fixed nitrogen into the atmosphere use the oxidizing power of NO to activate inert ammonium into hydrazine (N2H4). Here, we describe an enzyme from the anammox bacterium Kuenenia stuttgartiensis that uses a novel pathway to make NO from hydroxylamine. This new enzyme is related to octaheme hydroxylamine oxidoreductase (HAO), a key protein in aerobic ammonium-oxidizing bacteria. By a multiphasic approach including the determination of the crystal structure of the K. stuttgartiensis enzyme at 1.8Angstrom resolution and refinement and reassessment of the HAO structure from Nitrosomonas europaea, both in the presence and absence of their substrates, we propose a model for NO formation by the K. stuttgartiensis enzyme. Our results expand the understanding of the functions that the widespread family of octaheme proteins have.
Structural basis of biological NO generation by octaheme oxidoreductases.,Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B J Biol Chem. 2013 Dec 3. PMID:24302732[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kartal B, Maalcke WJ, de Almeida NM, Cirpus I, Gloerich J, Geerts W, Op den Camp HJ, Harhangi HR, Janssen-Megens EM, Francoijs KJ, Stunnenberg HG, Keltjens JT, Jetten MS, Strous M. Molecular mechanism of anaerobic ammonium oxidation. Nature. 2011 Oct 2;479(7371):127-30. doi: 10.1038/nature10453. PMID:21964329 doi:http://dx.doi.org/10.1038/nature10453
- ↑ Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B. Structural basis of biological NO generation by octaheme oxidoreductases. J Biol Chem. 2013 Dec 3. PMID:24302732 doi:http://dx.doi.org/10.1074/jbc.M113.525147
- ↑ Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B. Structural basis of biological NO generation by octaheme oxidoreductases. J Biol Chem. 2013 Dec 3. PMID:24302732 doi:http://dx.doi.org/10.1074/jbc.M113.525147
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