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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.
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: 2019-07-23bibliografisk kontrollert

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