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Functional interact...
Functional interactions between nitrite reductase and nitric oxide reductase from Paracoccus denitrificans
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- Albertsson, Ingrid (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, SE-10691 Stockholm, Sweden.
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- Sjöholm, Johannes (författare)
- Stockholms universitet,KTH,Tillämpad fysik,Institutionen för biokemi och biofysik,Royal Institute of Technology (KTH), Sweden
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- ter Beek, Josy (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, SE-10691 Stockholm, Sweden.;Umea Univ, Dept Med Biochem & Biophys, SE-90187 Umea, Sweden.
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- Watmough, Nicholas J. (författare)
- Univ East Anglia, Sch Biol Sci, Norwich Res Pk, Norwich NR4 7TJ, Norfolk, England.
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- Widengren, Jerker (författare)
- KTH,Tillämpad fysik
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- Ädelroth, Pia (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Stockholm Univ, Dept Biochem & Biophys, Svante Arrhenius Vag 16C, SE-10691 Stockholm, Sweden.
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(creator_code:org_t)
- 2019-11-21
- 2019
- Engelska.
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Ingår i: Scientific Reports. - : Nature Publishing Group. - 2045-2322. ; 9
- Relaterad länk:
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https://doi.org/10.1...
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https://www.nature.c...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- Denitrification is a microbial pathway that constitutes an important part of the nitrogen cycle on earth. Denitrifying organisms use nitrate as a terminal electron acceptor and reduce it stepwise to nitrogen gas, a process that produces the toxic nitric oxide (NO) molecule as an intermediate. In this work, we have investigated the possible functional interaction between the enzyme that produces NO; the cd(1) nitrite reductase (cd(1)NiR) and the enzyme that reduces NO; the c-type nitric oxide reductase (cNOR), from the model soil bacterium P. denitrificans. Such an interaction was observed previously between purified components from P. aeruginosa and could help channeling the NO (directly from the site of formation to the side of reduction), in order to protect the cell from this toxic intermediate. We find that electron donation to cNOR is inhibited in the presence of cd(1)NiR, presumably because cd(1)NiR binds cNOR at the same location as the electron donor. We further find that the presence of cNOR influences the dimerization of cd(1)NiR. Overall, although we find no evidence for a high-affinity, constant interaction between the two enzymes, our data supports transient interactions between cd(1)NiR and cNOR that influence enzymatic properties of cNOR and oligomerization properties of cd(1)NiR. We speculate that this could be of particular importance in vivo during metabolic switches between aerobic and denitrifying conditions.
Ämnesord
- NATURVETENSKAP -- Fysik (hsv//swe)
- NATURAL SCIENCES -- Physical Sciences (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
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- ref (ämneskategori)
- art (ämneskategori)
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