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  Characterization of anammox hydrazine dehydrogenase, a key N2-producing enzyme in the global nitrogen cycle

Maalcke, W. J., Reimann, J., de Vries, S., Butt, J. N., Dietl, A., Kip, N., et al. (2016). Characterization of anammox hydrazine dehydrogenase, a key N2-producing enzyme in the global nitrogen cycle. The Journal of Biological Chemistry, 291: jbc.M116.735530, pp. 17077-17092. doi:10.1074/jbc.M116.735530.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-ECE7-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-9CDF-6
Genre: Journal Article

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 Creators:
Maalcke, Wouter J., Author
Reimann, Joachim, Author
de Vries, Simon, Author
Butt, Julea N., Author
Dietl, Andreas1, Author              
Kip, Nardy, Author
Mersdorf, Ulrike1, Author              
Barends, Thomas R.M.1, Author              
Jetten, Mike S.M., Author
Keltjens, Jan T., Author
Kartal, Boran, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: anammox, hydrazine, hydroxylamine oxidoreductase, Kuenenia stuttgartiensis. multiheme proteins, nitrogen cycle. electron paramagnetic resonance (EPR), enzyme kinetics, enzyme purification, nitrogen metabolism, reactive nitrogen species (RNS), Anaerobic Ammonium Oxidation, octaheme proteins
 Abstract: Anaerobic ammonium-oxidizing (anammox) bacteria derive their energy for growth from the oxidation of ammonium with nitrite as the electron acceptor. N2, the end product of this metabolism, is produced from the oxidation of the intermediate, hydrazine (N2H4). Previously, we identified N2-producing hydrazine dehydrogenase (KsHDH) from the anammox organism Kuenenia stuttgartiensis as the gene product of kustc0694 and determined some of its catalytic properties. In the genome of K. stuttgartiensis, kustc0694 is one out of ten paralogs related to octaheme hydroxylamine (NH2OH) oxidoreductase (HAO). Here, we characterized KsHDH as a covalently cross-linked homotrimeric octaheme protein as found for HAO and HAO-related hydroxylamine-oxidizing enzyme kustc1061 (KsHOX) from K. stuttgartiensis. Interestingly, the HDH trimers formed octamers in solution, each octamer harboring an amazing 192 c-type heme moieties. While HAO and KsHOX are capable of hydrazine oxidation as well, KsHDH was highly specific for this activity. To understand this specificity, we performed detailed amino acid sequence analyses and investigated the catalytic and spectroscopic (electronic absorbance, EPR) properties of KsHDH in comparison with the well-defined HAO and HOX. We conclude that HDH specificity is most likely derived from structural changes around the catalytic heme 4 (P460) and of the electron-wiring circuit comprising seven His/His-ligated c-type hemes in each subunit. These nuances make HDH a globally prominent N2-producing enzyme, next to nitrous oxide (N2O) reductase from denitrifying microorganisms.

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Language(s): eng - English
 Dates: 2016-04-282016-06-172016-06-172016-08-12
 Publication Status: Published in print
 Pages: 21
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 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: 291 Sequence Number: jbc.M116.735530 Start / End Page: 17077 - 17092 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1