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-Structure paper
タイトル | A 192-heme electron transfer network in the hydrazine dehydrogenase complex. |
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ジャーナル・号・ページ | Sci Adv, Vol. 5, Issue 4, Page eaav4310, Year 2019 |
掲載日 | 2019年4月17日 |
![]() | M Akram / A Dietl / U Mersdorf / S Prinz / W Maalcke / J Keltjens / C Ferousi / N M de Almeida / J Reimann / B Kartal / M S M Jetten / K Parey / T R M Barends / ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 2.8 - 6.2 Å |
構造データ | ![]() EMDB-0205: ![]() EMDB-0206: ![]() EMDB-0207: ![]() PDB-6hif: |
化合物 | ![]() ChemComp-HEC: ![]() ChemComp-SO4: ![]() ChemComp-GOL: ![]() ChemComp-K: ![]() ChemComp-HOH: |
由来 |
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![]() | OXIDOREDUCTASE / anammox / hydrazine / dehydrogenase / P460 / redox |