دورية أكاديمية
أعرض في EDS

A 192-heme electron transfer network in the hydrazine dehydrogenase complex.

التفاصيل البيبلوغرافية
العنوان: A 192-heme electron transfer network in the hydrazine dehydrogenase complex.
المؤلفون: Akram M; Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany., Dietl A; Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany., Mersdorf U; Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany., Prinz S; Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany., Maalcke W; Department of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands., Keltjens J; Department of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands., Ferousi C; Department of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands., de Almeida NM; Department of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands., Reimann J; Department of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands., Kartal B; Department of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands., Jetten MSM; Department of Microbiology, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, Netherlands., Parey K; Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany., Barends TRM; Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany.
المصدر: Science advances [Sci Adv] 2019 Apr 17; Vol. 5 (4), pp. eaav4310. Date of Electronic Publication: 2019 Apr 17 (Print Publication: 2019).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 101653440 Publication Model: eCollection Cited Medium: Internet ISSN: 2375-2548 (Electronic) Linking ISSN: 23752548 NLM ISO Abbreviation: Sci Adv Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Association for the Advancement of Science, [2015]-
مواضيع طبية MeSH: Bacterial Proteins/*chemistry , Heme/*chemistry , Oxidoreductases/*chemistry, Bacterial Proteins/metabolism ; Binding Sites ; Catalytic Domain ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Electron Transport ; Gram-Negative Bacteria/enzymology ; Oxidoreductases/metabolism ; Protein Structure, Quaternary
مستخلص: 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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المشرفين على المادة: 0 (Bacterial Proteins)
42VZT0U6YR (Heme)
EC 1.- (Oxidoreductases)
تواريخ الأحداث: Date Created: 20190420 Date Completed: 20200427 Latest Revision: 20200427
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC6469936
DOI: 10.1126/sciadv.aav4310
PMID: 31001586
قاعدة البيانات: MEDLINE
الوصف
تدمد:2375-2548
DOI:10.1126/sciadv.aav4310