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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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Chicano, Tadeo Moreno1, Author
Dietrich, Lea2, Author           
de Almeida, Naomi M.3, Author
Akram, Mohd1, Author
Hartmann, Elisabeth1, Author
Leidreiter, Franziska1, Author
Leopoldus, Daniel1, Author
Mueller, Melanie1, Author
Sanchez, Ricardo M.4, 5, Author           
Nuijten, Guylaine H. L.3, Author
Reimann, Joachim3, Author
Seifert, Kerstin-Anikó1, Author
Schlichting, Ilme1, Author
van Niftrik, Laura3, Author
Jetten, Mike S. M.3, Author
Dietl, Andreas1, Author
Kartal, Boran6, 7, Author
Parey, Kristian2, Author           
Barends, Thomas R. M.1, Author
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Heidelberg, Germany, ou_persistent22              
2Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
3Department of Microbiology, Radboud University, Nijmegen, the Netherlands, ou_persistent22              
4Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society, ou_2253651              
5Buchmann Institute for Molecular Life Sciences, Goethe University of Frankfurt am Main, Frankfurt am Main, Germany, ou_persistent22              
6Microbial Physiology Group, Max Planck Institute for Marine Microbiology, Bremen, Germany, ou_persistent22              
7Department of Life Science and Chemistry, Jacobs University Bremen, Bremen, Germany, ou_persistent22              


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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.


Language(s): eng - English
 Dates: 2021-01-112021-06-102021-07-152021-09
 Publication Status: Published in print
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41564-021-00934-8
BibTex Citekey: chicano_structural_2021
 Degree: -



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Title: Nature Microbiology
  Abbreviation : Nat. Microbiol.
Source Genre: Journal
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