Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6HIF

Kuenenia stuttgartiensis hydrazine dehydrogenase complex

This is a non-PDB format compatible entry.
Summary for 6HIF
Entry DOI10.2210/pdb6hif/pdb
EMDB information0205 0206
DescriptorHydrazine dehydrogenase, hdh assembly factor Kustc1130, HEME C, ... (7 entities in total)
Functional Keywordsanammox, hydrazine, dehydrogenase, p460, redox, oxidoreductase
Biological sourceKuenenia stuttgartiensis
More
Total number of polymer chains36
Total formula weight1846125.04
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 citationAkram, 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: 31001586
DOI: 10.1126/sciadv.aav4310
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon