6hif: Difference between revisions
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==Kuenenia stuttgartiensis hydrazine dehydrogenase complex== | |||
<StructureSection load='6hif' size='340' side='right'caption='[[6hif]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== 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> | |||
</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> | |||
[[Category: | <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> | ||
[[Category: | <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> | ||
</table> | |||
== 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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hydrazine dehydrogenase]] | |||
[[Category: Kuenenia stuttgartiensis]] | |||
[[Category: Large Structures]] | |||
[[Category: Akram, M]] | |||
[[Category: Almeida, N M.de]] | |||
[[Category: Barends, T R.M]] | |||
[[Category: Dietl, A]] | |||
[[Category: Ferousi, C]] | [[Category: Ferousi, C]] | ||
[[Category: | [[Category: Jetten, M S.M]] | ||
[[Category: Kartal, B]] | |||
[[Category: Keltjens, J]] | |||
[[Category: Maalcke, W]] | [[Category: Maalcke, W]] | ||
[[Category: Mersdorf, U]] | [[Category: Mersdorf, U]] | ||
[[Category: Parey, K]] | [[Category: Parey, K]] | ||
[[Category: | [[Category: Prinz, S]] | ||
[[Category: | [[Category: Reimann, J]] | ||
[[Category: Anammox]] | |||
[[Category: Dehydrogenase]] | |||
[[Category: Hydrazine]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: P460]] | |||
[[Category: Redox]] |
Revision as of 08:57, 17 April 2019
Kuenenia stuttgartiensis hydrazine dehydrogenase complexKuenenia stuttgartiensis hydrazine dehydrogenase complex
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] References
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