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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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Main Authors: | , , , |
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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 |