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Insights into the mechanism of nitric oxide reductase from a Fe-B-depleted variant
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för organisk kemi.ORCID-id: 0000-0003-0702-7831
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Rekke forfattare: 42019 (engelsk)Inngår i: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 593, nr 12, s. 1351-1359Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

A key step of denitrification, the reduction of toxic nitric oxide to nitrous oxide, is catalysed by cytochrome c-dependent NO reductase (cNOR). cNOR contains four redox-active cofactors: three hemes and a nonheme iron (Fe-B). Heme b(3) and Fe-B constitute the active site, but the specific mechanism of NO-binding events and reduction is under debate. Here, we used a recently constructed, fully folded and hemylated cNOR variant that lacks Fe-B to investigate the role of Fe-B during catalysis. We show that in the Fe-B-less cNOR, binding of both NO and O-2 to heme b(3) still occurs but further reduction is impaired, although to a lesser degree for O-2 than for NO. Implications for the catalytic mechanisms of cNOR are discussed.

sted, utgiver, år, opplag, sider
2019. Vol. 593, nr 12, s. 1351-1359
Emneord [en]
enzymatic mechanism, NO reduction, non-heme iron, O-2 reduction
HSV kategori
Identifikatorer
URN: urn:nbn:se:su:diva-170880DOI: 10.1002/1873-3468.13436ISI: 000472673700008PubMedID: 31077353OAI: oai:DiVA.org:su-170880DiVA, id: diva2:1338523
Tilgjengelig fra: 2019-07-23 Laget: 2019-07-23 Sist oppdatert: 2020-02-06bibliografisk kontrollert

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