Bioinspired electrocatalytic reduction of nitric oxide by immobilized heme groups

M.T. Groot, de; M. Merkx; M.T.M. Koper

doi:10.1016/j.crci.2006.11.005

Bioinspired electrocatalytic reduction of nitric oxide by immobilized heme groups

M.T. Groot, de, M. Merkx, M.T.M. Koper

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

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Abstract

This paper discusses our work on the redn. of nitric oxide (NO) by heme groups immobilized on electrode surfaces, which has been conducted in search for selective NO redn. catalysts. Results show two redn. pathways, one leading to the formation of N2O and another leading to the formation of NH2OH. By changing the conditions (pH, potential, NO concn. and immobilization method), 100% selectivity toward either N2O or NH2OH can be obtained. A difference compared to NO reducing enzymes and metals is that immobilized heme groups do not reduce NH2OH further to NH3. Apparently, binding to an isolated heme group is insufficient to break the N-O bond. [on SciFinder (R)]

Original language	English
Pages (from-to)	414-420
Journal	Comptes Rendus Chimie
Volume	10
Issue number	4-5
DOIs	https://doi.org/10.1016/j.crci.2006.11.005
Publication status	Published - 2007

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10.1016/j.crci.2006.11.005

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title = "Bioinspired electrocatalytic reduction of nitric oxide by immobilized heme groups",

abstract = "This paper discusses our work on the redn. of nitric oxide (NO) by heme groups immobilized on electrode surfaces, which has been conducted in search for selective NO redn. catalysts. Results show two redn. pathways, one leading to the formation of N2O and another leading to the formation of NH2OH. By changing the conditions (pH, potential, NO concn. and immobilization method), 100% selectivity toward either N2O or NH2OH can be obtained. A difference compared to NO reducing enzymes and metals is that immobilized heme groups do not reduce NH2OH further to NH3. Apparently, binding to an isolated heme group is insufficient to break the N-O bond. [on SciFinder (R)]",

author = "{Groot, de}, M.T. and M. Merkx and M.T.M. Koper",

year = "2007",

doi = "10.1016/j.crci.2006.11.005",

language = "English",

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journal = "Comptes Rendus Chimie",

issn = "1631-0748",

publisher = "Elsevier B.V.",

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TY - JOUR

T1 - Bioinspired electrocatalytic reduction of nitric oxide by immobilized heme groups

AU - Groot, de, M.T.

AU - Merkx, M.

AU - Koper, M.T.M.

PY - 2007

Y1 - 2007

N2 - This paper discusses our work on the redn. of nitric oxide (NO) by heme groups immobilized on electrode surfaces, which has been conducted in search for selective NO redn. catalysts. Results show two redn. pathways, one leading to the formation of N2O and another leading to the formation of NH2OH. By changing the conditions (pH, potential, NO concn. and immobilization method), 100% selectivity toward either N2O or NH2OH can be obtained. A difference compared to NO reducing enzymes and metals is that immobilized heme groups do not reduce NH2OH further to NH3. Apparently, binding to an isolated heme group is insufficient to break the N-O bond. [on SciFinder (R)]

AB - This paper discusses our work on the redn. of nitric oxide (NO) by heme groups immobilized on electrode surfaces, which has been conducted in search for selective NO redn. catalysts. Results show two redn. pathways, one leading to the formation of N2O and another leading to the formation of NH2OH. By changing the conditions (pH, potential, NO concn. and immobilization method), 100% selectivity toward either N2O or NH2OH can be obtained. A difference compared to NO reducing enzymes and metals is that immobilized heme groups do not reduce NH2OH further to NH3. Apparently, binding to an isolated heme group is insufficient to break the N-O bond. [on SciFinder (R)]

U2 - 10.1016/j.crci.2006.11.005

DO - 10.1016/j.crci.2006.11.005

M3 - Article

SN - 1631-0748

VL - 10

SP - 414

EP - 420

JO - Comptes Rendus Chimie

JF - Comptes Rendus Chimie

IS - 4-5

ER -

Bioinspired electrocatalytic reduction of nitric oxide by immobilized heme groups

Abstract

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