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  Structural and functional characterization of the intracellular filament-forming nitrite oxidoreductase multiprotein complex

Chicano, T. M., Dietrich, L., de Almeida, N. M., Akram, M., Hartmann, E., Leidreiter, F., et al. (2021). Structural and functional characterization of the intracellular filament-forming nitrite oxidoreductase multiprotein complex. Nature Microbiology, 6(9), 1129-1139. doi:10.1038/s41564-021-00934-8.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0008-E43C-4 Version Permalink: https://hdl.handle.net/21.11116/0000-0009-6A96-7
Genre: Journal Article

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Chicano, Tadeo Moreno1, Author           
Dietrich, Lea, Author           
de Almeida, Naomi M., Author
Akram, Mohd1, Author           
Hartmann, Elisabeth1, Author           
Leidreiter, Franziska1, Author           
Leopoldus, Daniel1, Author           
Müller, Melanie1, Author           
Sanchez, Ricardo M., Author           
Nuijten, Guylaine H. L., Author
Reimann, Joachim, Author
Seifert, Kerstin-Anikó1, Author           
Schlichting, Ilme1, Author           
van Niftrik, Laura, Author
Jetten, Mike S. M., Author
Dietl, Andreas1, Author           
Kartal, Boran, Author
Parey, Kristian, Author           
Barends, Thomas R. M.1, Author           
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: Nitrate is an abundant nutrient and electron acceptor throughout Earth's biosphere. Virtually all nitrate in nature is produced by the oxidation of nitrite by the nitrite oxidoreductase (NXR) multiprotein complex. NXR is a crucial enzyme in the global biological nitrogen cycle, and is found in nitrite-oxidizing bacteria (including comammox organisms), which generate the bulk of the nitrate in the environment, and in anaerobic ammonium-oxidizing (anammox) bacteria which produce half of the dinitrogen gas in our atmosphere. However, despite its central role in biology and decades of intense study, no structural information on NXR is available. Here, we present a structural and biochemical analysis of the NXR from the anammox bacterium Kuenenia stuttgartiensis, integrating X-ray crystallography, cryo-electron tomography, helical reconstruction cryo-electron microscopy, interaction and reconstitution studies and enzyme kinetics. We find that NXR catalyses both nitrite oxidation and nitrate reduction, and show that in the cell, NXR is arranged in tubules several hundred nanometres long. We reveal the tubule architecture and show that tubule formation is induced by a previously unidentified, haem-containing subunit, NXR-T. The results also reveal unexpected features in the active site of the enzyme, an unusual cofactor coordination in the protein's electron transport chain, and elucidate the electron transfer pathways within the complex.

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Language(s): eng - English
 Dates: 2021-01-112021-06-102021-07-152021-09-01
 Publication Status: Issued
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41564-021-00934-8
BibTex Citekey: chicano_structural_2021
URI: https://pubmed.ncbi.nlm.nih.gov/34267357/
 Degree: -

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Title: Nature Microbiology
  Abbreviation : Nat. Microbiol.
Source Genre: Journal
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Affiliations:
Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 6 (9) Sequence Number: - Start / End Page: 1129 - 1139 Identifier: Other: 2058-5276
CoNE: https://pure.mpg.de/cone/journals/resource/2058-5276