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/Cu_B center of ba₃-cytochrome c oxidase as determined by resonance Raman spectroscopy

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

Department of Chemical Sciences

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	286-289
Number of pages	4
Journal	Chemical Communications
Volume	51
Issue number	2
DOIs	https://doi.org/10.1039/c4cc08019j
Publication status	Published - 7 Jan 2015

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title = "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.",

author = "Andreas Loullis and Noor, {Mohamed Radzi} and Tewfik Soulimane and Eftychia Pinakoulaki",

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AU - Noor, Mohamed Radzi

AU - Soulimane, Tewfik

AU - Pinakoulaki, Eftychia

PY - 2015/1/7

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N2 - 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.

AB - 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.

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The structure of a ferrous heme-nitro species in the binuclear heme a₃/Cu_B center of ba₃-cytochrome c oxidase as determined by resonance Raman spectroscopy

Abstract

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