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| | <StructureSection load='6hif' size='340' side='right'caption='[[6hif]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='6hif' size='340' side='right'caption='[[6hif]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hif]] is a 36 chain structure with sequence from [http://en.wikipedia.org/wiki/Kuenenia_stuttgartiensis Kuenenia stuttgartiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HIF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HIF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hif]] is a 36 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=6HIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HIF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrazine_dehydrogenase Hydrazine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.7.2.8 1.7.2.8] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6hif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hif OCA], [http://pdbe.org/6hif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hif RCSB], [http://www.ebi.ac.uk/pdbsum/6hif PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hif ProSAT]</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=6hif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hif OCA], [https://pdbe.org/6hif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hif RCSB], [https://www.ebi.ac.uk/pdbsum/6hif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hif ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HDH_KUEST HDH_KUEST]] Catalyzes the four-electron oxidation of hydrazine to N2 (PubMed:21964329). The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799). Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329). Cannot oxidize hydroxylamine to NO (PubMed:21964329).<ref>PMID:21964329</ref> <ref>PMID:23210799</ref> | + | [https://www.uniprot.org/uniprot/HDH_KUEST HDH_KUEST] Catalyzes the four-electron oxidation of hydrazine to N2 (PubMed:21964329). The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799). Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329). Cannot oxidize hydroxylamine to NO (PubMed:21964329).<ref>PMID:21964329</ref> <ref>PMID:23210799</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hydrazine dehydrogenase]] | + | [[Category: Candidatus Kuenenia stuttgartiensis]] |
| - | [[Category: Kuenenia stuttgartiensis]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Akram, M]] | + | [[Category: Akram M]] |
| - | [[Category: Almeida, N M.de]]
| + | [[Category: Barends TRM]] |
| - | [[Category: Barends, T R.M]] | + | [[Category: Dietl A]] |
| - | [[Category: Dietl, A]] | + | [[Category: Ferousi C]] |
| - | [[Category: Ferousi, C]] | + | [[Category: Jetten MSM]] |
| - | [[Category: Jetten, M S.M]] | + | [[Category: Kartal B]] |
| - | [[Category: Kartal, B]] | + | [[Category: Keltjens J]] |
| - | [[Category: Keltjens, J]] | + | [[Category: Maalcke W]] |
| - | [[Category: Maalcke, W]] | + | [[Category: Mersdorf U]] |
| - | [[Category: Mersdorf, U]] | + | [[Category: Parey K]] |
| - | [[Category: Parey, K]] | + | [[Category: Prinz S]] |
| - | [[Category: Prinz, S]] | + | [[Category: Reimann J]] |
| - | [[Category: Reimann, J]] | + | [[Category: De Almeida NM]] |
| - | [[Category: Anammox]] | + | |
| - | [[Category: Dehydrogenase]]
| + | |
| - | [[Category: Hydrazine]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: P460]]
| + | |
| - | [[Category: Redox]]
| + | |
| Structural highlights
Function
HDH_KUEST Catalyzes the four-electron oxidation of hydrazine to N2 (PubMed:21964329). The electrons derived from hydrazine oxidation may be transferred to the quinone pool and exploited to promote the generation of proton-motive force (pmf) across the anammoxosome membrane (PubMed:21964329, PubMed:23210799). Is involved in anaerobic ammonium oxidation (anammox), a biological process in which nitrite is used as the electron acceptor in the conversion of ammonium to dinitrogen gas (N2) and water; this bacterial process has a major role in the Earth's nitrogen cycle and has been estimated to synthesize up to 50% of the dinitrogen gas emitted into our atmosphere from the oceans (PubMed:21964329). Cannot oxidize hydroxylamine to NO (PubMed:21964329).[1] [2]
Publication Abstract from PubMed
Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas and water through the highly reactive intermediate hydrazine. So far, it is unknown how anammox organisms convert the toxic hydrazine into nitrogen and harvest the extremely low potential electrons (-750 mV) released in this process. We report the crystal structure and cryo electron microscopy structures of the responsible enzyme, hydrazine dehydrogenase, which is a 1.7 MDa multiprotein complex containing an extended electron transfer network of 192 heme groups spanning the entire complex. This unique molecular arrangement suggests a way in which the protein stores and releases the electrons obtained from hydrazine conversion, the final step in the globally important anammox process.
A 192-heme electron transfer network in the hydrazine dehydrogenase complex.,Akram M, Dietl A, Mersdorf U, Prinz S, Maalcke W, Keltjens J, Ferousi C, de Almeida NM, Reimann J, Kartal B, Jetten MSM, Parey K, Barends TRM Sci Adv. 2019 Apr 17;5(4):eaav4310. doi: 10.1126/sciadv.aav4310. eCollection 2019, Apr. PMID:31001586[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
- ↑ Kartal B, de Almeida NM, Maalcke WJ, Op den Camp HJ, Jetten MS, Keltjens JT. How to make a living from anaerobic ammonium oxidation. FEMS Microbiol Rev. 2013 May;37(3):428-61. doi: 10.1111/1574-6976.12014. Epub, 2013 Jan 21. PMID:23210799 doi:http://dx.doi.org/10.1111/1574-6976.12014
- ↑ Akram M, Dietl A, Mersdorf U, Prinz S, Maalcke W, Keltjens J, Ferousi C, de Almeida NM, Reimann J, Kartal B, Jetten MSM, Parey K, Barends TRM. A 192-heme electron transfer network in the hydrazine dehydrogenase complex. Sci Adv. 2019 Apr 17;5(4):eaav4310. doi: 10.1126/sciadv.aav4310. eCollection 2019, Apr. PMID:31001586 doi:http://dx.doi.org/10.1126/sciadv.aav4310
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