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

Andreas Loullis; Mohamed Radzi Noor; Tewfik Soulimane; Eftychia Pinakoulaki

doi:10.1039/c4cc08019j

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

Chem Commun (Camb). 2015;51(2):286-9. doi: 10.1039/c4cc08019j. Epub 2014 Nov 18.

Authors

Andreas Loullis¹, Mohamed Radzi Noor, Tewfik Soulimane, Eftychia Pinakoulaki

Affiliation

¹ Department of Chemistry, University of Cyprus, PO Box 20537, 1678, Nicosia, Cyprus. effiep@ucy.ac.cy.

PMID: 25406996
DOI: 10.1039/c4cc08019j

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / chemistry*
Copper / chemistry
Cytochrome b Group / chemistry*
Electron Transport Complex IV / chemistry*
Heme / analogs & derivatives*
Heme / chemistry
Models, Molecular
Nitrites / chemistry
Spectrum Analysis, Raman
Thermus thermophilus / chemistry*

Substances

Bacterial Proteins
Cytochrome b Group
Nitrites
heme a
Heme
Copper
cytochrome ba3
Electron Transport Complex IV