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Epsilonproteobacterial hydroxylamine oxidoreductase (εHao): Characterization of a 'missing link' in the multihaem cytochrome c family.

Haase, Doreen ; Hermann, Bianca ; Einsle, Oliver ; Simon, Jörg :
Epsilonproteobacterial hydroxylamine oxidoreductase (εHao): Characterization of a 'missing link' in the multihaem cytochrome c family.
In: Molecular microbiology, 105 (1) pp. 127-138. ISSN 1365-2958
[Artikel], (2017)

Kurzbeschreibung (Abstract)

Members of the multihaem cytochrome c (MCC) family such as pentahaem cytochrome c nitrite reductase (NrfA) or octahaem hydroxylamine oxidoreductase (Hao) are involved in various microbial respiratory electron transport chains. Some members of the Hao subfamily, here called εHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Here, εHao proteins from the host-associated Epsilonproteobacteria Campylobacter fetus and Campylobacter curvus and the deep-sea hydrothermal vent bacteria Caminibacter mediatlanticus and Nautilia profundicola were purified as εHao-maltose binding protein fusions produced in Wolinella succinogenes. All four proteins were able to catalyse reduction of nitrite (yielding ammonium) and hydroxylamine whereas hydroxylamine oxidation was negligible. The introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins did neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm. In most cases, the εHao-encoding gene haoA was situated downstream of haoB, which predicts a tetrahaem cytochrome c of the NapC/NrfH family. This suggested the formation of a membrane-bound HaoBA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. The results indicate that εHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a 'missing link' in the evolution of NrfA and Hao enzymes. This article is protected by copyright. All rights reserved.

Typ des Eintrags: Artikel
Erschienen: 2017
Autor(en): Haase, Doreen ; Hermann, Bianca ; Einsle, Oliver ; Simon, Jörg
Titel: Epsilonproteobacterial hydroxylamine oxidoreductase (εHao): Characterization of a 'missing link' in the multihaem cytochrome c family.
Sprache: Englisch
Kurzbeschreibung (Abstract):

Members of the multihaem cytochrome c (MCC) family such as pentahaem cytochrome c nitrite reductase (NrfA) or octahaem hydroxylamine oxidoreductase (Hao) are involved in various microbial respiratory electron transport chains. Some members of the Hao subfamily, here called εHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Here, εHao proteins from the host-associated Epsilonproteobacteria Campylobacter fetus and Campylobacter curvus and the deep-sea hydrothermal vent bacteria Caminibacter mediatlanticus and Nautilia profundicola were purified as εHao-maltose binding protein fusions produced in Wolinella succinogenes. All four proteins were able to catalyse reduction of nitrite (yielding ammonium) and hydroxylamine whereas hydroxylamine oxidation was negligible. The introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins did neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm. In most cases, the εHao-encoding gene haoA was situated downstream of haoB, which predicts a tetrahaem cytochrome c of the NapC/NrfH family. This suggested the formation of a membrane-bound HaoBA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. The results indicate that εHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a 'missing link' in the evolution of NrfA and Hao enzymes. This article is protected by copyright. All rights reserved.

Titel der Zeitschrift, Zeitung oder Schriftenreihe: Molecular microbiology
Band: 105
(Heft-)Nummer: 1
Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Microbial Energy Conversion and Biotechnology
Hinterlegungsdatum: 11 Apr 2017 09:48
ID-Nummer: pmid:28388834
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