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

Akram, M., Dietl, A., Mersdorf, U., Prinz, S., Maalcke, W. J., Keltjens, J. T., et al. (2019). A 192-heme electron transfer network in the hydrazine dehydrogenase complex. Science Advances, 5(4): eaav4310, pp. 1-8. doi:10.1126/sciadv.aav4310.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-9F4E-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-9F4F-3
Genre: Journal Article

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SciAdv_5_2019_eaav4310.pdf (Any fulltext), 7MB
 
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 Creators:
Akram, Mohd1, Author              
Dietl, Andreas1, Author              
Mersdorf, Ulli1, Author              
Prinz , Simone, Author
Maalcke, Wouter J., Author
Keltjens, Jan T., Author
Ferousi, Christina, Author
de Almeida, Naomi M., Author
Reimann, J., Author
Kartal, Boran, Author
Jetten, Mike S. M., Author
Parey, Kristian, Author
Barends, Thomas1, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Anaerobic ammonium oxidation (anammox) is a major process in the biogeochemical nitrogen cycle in which nitrite and ammonium are converted to dinitrogen gas andwater 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 1.7MDa multiprotein complex containing an extended electron transfer network of 192 heme groups spanning the entire complex. This unique molecular arrangement suggests a way inwhich the protein stores and releases the electrons obtained from hydrazine conversion, the final step in the globally important anammox process.

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Language(s): eng - English
 Dates: 2018-09-142019-02-282019-04-172019-04-17
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1126/sciadv.aav4310
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Title: Science Advances
  Other : Sci. Adv.
Source Genre: Journal
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Publ. Info: Washington : AAAS
Pages: - Volume / Issue: 5 (4) Sequence Number: eaav4310 Start / End Page: 1 - 8 Identifier: ISSN: 2375-2548
CoNE: https://pure.mpg.de/cone/journals/resource/2375-2548