6HIF
Kuenenia stuttgartiensis hydrazine dehydrogenase complex
This is a non-PDB format compatible entry.
Summary for 6HIF
Entry DOI | 10.2210/pdb6hif/pdb |
EMDB information | 0205 0206 |
Descriptor | Hydrazine dehydrogenase, hdh assembly factor Kustc1130, HEME C, ... (7 entities in total) |
Functional Keywords | anammox, hydrazine, dehydrogenase, p460, redox, oxidoreductase |
Biological source | Kuenenia stuttgartiensis More |
Total number of polymer chains | 36 |
Total formula weight | 1846125.04 |
Authors | Akram, M.,Dietl, A.,Mersdorf, U.,Prinz, S.,Maalcke, W.,Keltjens, J.,Ferousi, C.,de Almeida, N.M.,Reimann, J.,Kartal, B.,Jetten, M.S.M.,Parey, K.,Barends, T.R.M. (deposition date: 2018-08-29, release date: 2019-04-17, Last modification date: 2024-01-17) |
Primary citation | Akram, M.,Dietl, A.,Mersdorf, U.,Prinz, S.,Maalcke, W.,Keltjens, J.,Ferousi, C.,de Almeida, N.M.,Reimann, J.,Kartal, B.,Jetten, M.S.M.,Parey, K.,Barends, T.R.M. A 192-heme electron transfer network in the hydrazine dehydrogenase complex. Sci Adv, 5:eaav4310-eaav4310, 2019 Cited by PubMed Abstract: 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. PubMed: 31001586DOI: 10.1126/sciadv.aav4310 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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