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  A nitric oxide-binding heterodimeric cytochrome c complex from the anammox bacterium Kuenenia stuttgartiensis binds to hydrazine synthase

Akram, M., Reimann, J., Dietl, A., Menzel, A., Versantvoort, W., Kartal, B., et al. (2019). A nitric oxide-binding heterodimeric cytochrome c complex from the anammox bacterium Kuenenia stuttgartiensis binds to hydrazine synthase. The Journal of Biological Chemistry, e-pup(788), 1-29. doi:10.1074/jbc.RA119.008788.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0004-C1BE-C Version Permalink: http://hdl.handle.net/21.11116/0000-0004-C1BF-B
Genre: Journal Article

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 Creators:
Akram, Mohd1, 2, 3, Author              
Reimann, Joachim, Author
Dietl, Andreas1, 3, 4, 5, Author              
Menzel, Andreas, Author
Versantvoort, Wouter, Author
Kartal, Boran, Author
Jetten, Mike S.M., Author
Barends, Thomas1, 2, 3, 4, 5, 6, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Coherent diffractive imaging, Max Planck Institute for Medical Research, Max Planck Society, ou_1497692              
3Structural Biology of Elemental Cycles, Max Planck Institute for Medical Research, Max Planck Society, ou_2205646              
4Heme and Flavin Enzymes, Max Planck Institute for Medical Research, Max Planck Society, ou_1497715              
5Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society, ou_1856341              
6Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society, ou_1497728              

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Free keywords: cytochrome c, nitric oxide, redox, bacterial metabolism, crystal structure, UV-Vis spectroscopy, anaerobic ammonium oxidation (anammox), NaxLS, nitrogen cycle, electron transport
 Abstract: Anaerobic ammonium oxidation (anammox) is a microbial process responsible for significant nitrogen loss from the oceans and other ecosystems. The redox reactions at the heart of anammox are catalyzed by large multiheme enzyme complexes that rely on small cytochrome c proteins for electron shuttling. Among the most highly abundant of these cytochromes is a unique heterodimeric complex composed of class I and class II c-type cytochrome called NaxLS, which has distinctive biochemical and spectroscopic properties. Here, we present the 1.7 Å resolution crystal structure of this complex from the anammox organism Kuenenia stuttgartiensis (KsNaxLS). The structure reveals that the heme irons in each subunit exhibit a rare His/Cys ligation, which, as we show by substitution, causes the observed unusual spectral properties. Unlike its individual subunits, the KsNaxLS complex binds nitric oxide (NO) only at the distal heme side, forming 6cNO adducts. This is likely due to steric immobilization of the proximal heme binding motifs upon complex formation, a finding that may be of functional relevance, since NO is an intermediate in the central anammox metabolism. Pulldown experiments with K. stuttgartiensis cell-free extract showed that the KsNaxLS complex binds specifically to one of the central anammox enzyme complexes, hydrazine synthase, which uses NO as one of its substrates. It is therefore possible that the KsNaxLS complex plays a role in binding the volatile NO to retain it in the cell for transfer to hydrazine synthase. Alternatively, we propose that KsNaxLS may shuttle electrons to this enzyme complex.

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Language(s): eng - English
 Dates: 2019-09-22
 Publication Status: Published in print
 Pages: 29
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.RA119.008788
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: e-pup (788) Sequence Number: - Start / End Page: 1 - 29 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1