Nitrite catalyzes ferriheme protein reductive nitrosylation
Nitrite catalyzes ferriheme protein reductive nitrosylation
Nitrite ion is found to catalyze the NO reduction of met-hemoglobin and met-myoglobin in pH 7.0 buffered aqueous solution. The catalysis rate constants for these ferriheme proteins and for two water-soluble ferriheme model systems follow the same order as do the FeIII/II reduction potentials of the ferric nitrosyl complexes. This is consistent with a proposed mechanism occurring via outer sphere reduction of the FeIII(NO) center by NO2- to give the FeII(NO) product plus NO2. Although the first step is thermodynamically uphill, the NO2 generated would be rapidly trapped by excess NO to form N2O3, which would hydrolyze. We speculate that, if formed in the proximity of the protein, the strong nitrosating agent N2O3 could also result in protein modifications.
10510-10511
Fernandez, Bernadette O.
9890aabc-1fe6-4530-a51e-31182e537131
Ford, Peter C.
a752d252-18ac-4b00-8c4b-c36f28cf15df
3 September 2003
Fernandez, Bernadette O.
9890aabc-1fe6-4530-a51e-31182e537131
Ford, Peter C.
a752d252-18ac-4b00-8c4b-c36f28cf15df
Fernandez, Bernadette O. and Ford, Peter C.
(2003)
Nitrite catalyzes ferriheme protein reductive nitrosylation.
Journal of the American Chemical Society, 125 (35), .
(doi:10.1021/ja036693b).
Abstract
Nitrite ion is found to catalyze the NO reduction of met-hemoglobin and met-myoglobin in pH 7.0 buffered aqueous solution. The catalysis rate constants for these ferriheme proteins and for two water-soluble ferriheme model systems follow the same order as do the FeIII/II reduction potentials of the ferric nitrosyl complexes. This is consistent with a proposed mechanism occurring via outer sphere reduction of the FeIII(NO) center by NO2- to give the FeII(NO) product plus NO2. Although the first step is thermodynamically uphill, the NO2 generated would be rapidly trapped by excess NO to form N2O3, which would hydrolyze. We speculate that, if formed in the proximity of the protein, the strong nitrosating agent N2O3 could also result in protein modifications.
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Published date: 3 September 2003
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Local EPrints ID: 445699
URI: http://eprints.soton.ac.uk/id/eprint/445699
ISSN: 0002-7863
PURE UUID: fccab29c-7ddd-4c31-8d52-1a3d60ef7e8c
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Date deposited: 06 Jan 2021 17:41
Last modified: 06 Jun 2024 01:51
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Author:
Bernadette O. Fernandez
Author:
Peter C. Ford
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