Issue 2, 2015

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 spectroscopy

Abstract

Members of the cytochrome c oxidase family exhibit nitrite reductase activity. In this work, we have characterized a ferrous heme a3-nitro species in ba3-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.

Graphical abstract: 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 spectroscopy

Supplementary files

Article information

Article type
Communication
Submitted
10 Oct 2014
Accepted
10 Nov 2014
First published
10 Nov 2014

Chem. Commun., 2015,51, 286-289

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 spectroscopy

A. Loullis, M. R. Noor, T. Soulimane and E. Pinakoulaki, Chem. Commun., 2015, 51, 286 DOI: 10.1039/C4CC08019J

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