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  A 60-heme reductase complex from an anammox bacterium shows an extended electron transfer pathway

Dietl, A., Maalcke, W. J., Ferousi, C., Jetten, M. S. M., Kartal, B., & Barends, T. R. M. (in press). A 60-heme reductase complex from an anammox bacterium shows an extended electron transfer pathway. Acta Crystallographica Section D: Structural Biology, 75, 1-9. doi:10.1107/S2059798318017473.

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 Creators:
Dietl, Andreas1, Author              
Maalcke, Wouter J., Author
Ferousi, Christina, Author
Jetten, Mike S. M., Author
Kartal, Boran, 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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Free keywords: hydroxylamine oxidoreductase; anaerobic ammonium oxidation; electron transfer; anammox; heme; Kuenenia stuttgartiensis
 Abstract: The hydroxylamine oxidoreductase/hydrazine dehydrogenase (HAO/HDH) protein family constitutes an important group of octaheme cytochromes c (OCCs). The majority of these proteins form homotrimers, with their subunits being covalently attached to each other via a rare cross-link between the catalytic heme moiety and a conserved tyrosine residue in an adjacent subunit. This covalent cross-link has been proposed to modulate the active-site heme towards oxidative catalysis by distorting the heme plane. In this study, the crystal structure of a stable complex of an HAO homologue (KsHAOr) with its diheme cytochrome c redox partner (KsDH) from the anammox bacterium Kuenenia stuttgartiensis was determined. KsHAOr lacks the tyrosine cross-link and is therefore tuned to reductive catalysis. The molecular model of the KsHAOr–KsDH complex at 2.6 Å resolution shows a heterododecameric (α6β6) assembly, which was also shown to be the oligomeric state in solution by analytical ultracentrifugation and multi-angle static light scattering. The 60-heme-containing protein complex reveals a unique extended electron transfer pathway and provides deeper insights into catalysis and electron transfer in reductive OCCs.

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Language(s): eng - English
 Dates: 2018-09-082018-12-10
 Publication Status: Accepted / In Press
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1107/S2059798318017473
 Degree: -

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Title: Acta Crystallographica Section D: Structural Biology
  Abbreviation : Acta Cryst. D
Source Genre: Journal
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Publ. Info: Chester, England : International Union of Crystallography
Pages: - Volume / Issue: 75 Sequence Number: - Start / End Page: 1 - 9 Identifier: ISSN: 2059-7983
CoNE: https://pure.mpg.de/cone/journals/resource/2059-7983