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Electron/Proton Coupling in Bacterial Nitric Oxide Reductase during Reduction of Oxygen
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Ansvarlig organisasjon
2005 Inngår i: Biochemistry, Vol. 44, nr 31, s. 10711-10719Artikkel i tidsskrift (Fagfellevurdert) Published
sted, utgiver, år, opplag, sider
2005. Vol. 44, nr 31, s. 10711-10719
Identifikatorer
URN: urn:nbn:se:su:diva-25461OAI: oai:DiVA.org:su-25461DiVA, id: diva2:199751
Merknad
Part of urn:nbn:se:su:diva-8171Tilgjengelig fra: 2008-09-25 Laget: 2008-09-25bibliografisk kontrollert
Inngår i avhandling
1. Nitric Oxide Reductase from Paracoccus denitrificans: A Proton Transfer Pathway from the “Wrong” Side
Åpne denne publikasjonen i ny fane eller vindu >>Nitric Oxide Reductase from Paracoccus denitrificans: A Proton Transfer Pathway from the “Wrong” Side
2008 (engelsk)Doktoravhandling, med artikler (Annet vitenskapelig)
Abstract [en]

Denitrification is an anaerobic process performed by several soil bacteria as an alternative to aerobic respiration. A key-step in denitrification (the N-N-bond is made) is catalyzed by nitric oxide reductase (NOR); 2NO + 2e- + 2H+ → N2O + H2O. NOR from Paracoccus denitrificans is a member of the heme copper oxidase superfamily (HCuOs), where the mitochondrial cytochrome c oxidase is the classical example. NOR is situated in the cytoplasmic membrane and can, as a side reaction, catalyze the reduction of oxygen to water.

NORs have properties that make them divergent members of the HCuOs; the reactions they catalyze are not electrogenic and they do not pump protons. They also have five strictly conserved glutamates in their catalytic subunit (NorB) that are not conserved in the ‘classical’ HCuOs. It has been asked whether the protons used in the reaction really come from the periplasm and if so how do the protons proceed through the protein into the catalytic site?

In order to find out whether the protons are taken from the periplasm or the cytoplasm and in order to pinpoint the proton-route in NorB, we studied electron- and proton transfer during a single- as well as multiple turnovers, using time resolved optical spectroscopy. Wild type NOR and several variants of the five conserved glutamates were investigated in their solubilised form or/and reconstituted into vesicles.

The results demonstrate that protons needed for the reaction indeed are taken from the periplasm and that all but one of the conserved glutamates are crucial for the oxidative phase of the reaction that is limited by proton uptake to the active site.

In this thesis it is proposed, using a model of NorB, that two of the glutamates are located at the entrance of the proton pathway which also contains two of the other glutamates close to the active site.

sted, utgiver, år, opplag, sider
Stockholm: Institutionen för biokemi och biofysik, 2008. s. 113
Emneord
denitrification, nitric oxide reductase, heme copper oxidase superfamily, divergent member, proton transfer, electron transfer, single turnover, spectroscopy, periplasm, glutamate, proton pathway
HSV kategori
Forskningsprogram
biokemi
Identifikatorer
urn:nbn:se:su:diva-8171 (URN)978-91-7155-740-7 (ISBN)
Disputas
2008-10-17, Magnélisalen, Kemiska övnigslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00
Opponent
Veileder
Tilgjengelig fra: 2008-09-25 Laget: 2008-09-25 Sist oppdatert: 2015-09-24bibliografisk kontrollert

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