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Insights into the mechanism of nitric oxide reductase from a Fe-B-depleted variant
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Organic Chemistry.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 42019 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 593, no 12, p. 1351-1359Article in journal (Refereed) 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.

Place, publisher, year, edition, pages
2019. Vol. 593, no 12, p. 1351-1359
Keywords [en]
enzymatic mechanism, NO reduction, non-heme iron, O-2 reduction
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-170880DOI: 10.1002/1873-3468.13436ISI: 000472673700008PubMedID: 31077353OAI: oai:DiVA.org:su-170880DiVA, id: diva2:1338523
Available from: 2019-07-23 Created: 2019-07-23 Last updated: 2019-07-23Bibliographically approved

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Kahle, MaximilianBlomberg, Margareta R. A.Ädelroth, Pia
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