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The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopyElectronic supplementary information (ESI) available: Details of experimental methods and supplementary Fig. S1 and S2. See DOI: 10.1039/c4cc08019j

Members of the cytochrome c oxidase family exhibit nitrite reductase activity. In this work, we have characterized a ferrous heme a 3 -nitro species in ba 3 -oxidase by resonance Raman spectroscopy. This provides the first evidence for the structure of a nitrite-bound species in the binuclear heme/c...

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Bibliographic Details
Main Authors: Loullis, Andreas, Noor, Mohamed Radzi, Soulimane, Tewfik, Pinakoulaki, Eftychia
Format: Article
Language:English
Online Access:Get full text
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Summary:Members of the cytochrome c oxidase family exhibit nitrite reductase activity. In this work, we have characterized a ferrous heme a 3 -nitro species in ba 3 -oxidase by resonance Raman spectroscopy. This provides the first evidence for the structure of a nitrite-bound species in the binuclear heme/copper center of cytochrome c oxidases. We present resonance Raman evidence for the formation of a ferrous heme-nitro species in the binuclear heme/copper center of ba 3 -oxidase.
ISSN:1359-7345
1364-548X
DOI:10.1039/c4cc08019j