2003
DOI: 10.1016/s0020-1693(03)00037-9
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Binding of nitric oxide to water-soluble iron(III) porphyrins

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Cited by 10 publications
(25 citation statements)
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“…From a biological point of view, the nitrogen oxide donors, particularly the S-nitrosothiols, are more interesting for the regulation of nitric oxide-dependent physiological processes. The present work shows that the mechanism of NO donation by SNAP to iron-porphyrins is different from the binding of NO molecules dissolved in buffer [26][27][28], leading to a much faster and probably direct reductive nitrosylation. It is also shown that simple membrane models, such as micelles, can influence the equilibrium between porphyrin monomers and dimers and modify nitrosylation rates.…”
Section: Discussionmentioning
confidence: 63%
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“…From a biological point of view, the nitrogen oxide donors, particularly the S-nitrosothiols, are more interesting for the regulation of nitric oxide-dependent physiological processes. The present work shows that the mechanism of NO donation by SNAP to iron-porphyrins is different from the binding of NO molecules dissolved in buffer [26][27][28], leading to a much faster and probably direct reductive nitrosylation. It is also shown that simple membrane models, such as micelles, can influence the equilibrium between porphyrin monomers and dimers and modify nitrosylation rates.…”
Section: Discussionmentioning
confidence: 63%
“…This interaction is expected to influence axial ligation. Several studies of nitric oxide reactions with water soluble ironporphyrins have recently appeared using solutions equilibrated with NO gas under various partial pressures [15,17,26,28]. From a biological point of view, the nitrogen oxide donors, particularly the S-nitrosothiols, are more interesting for the regulation of nitric oxide-dependent physiological processes.…”
Section: Discussionmentioning
confidence: 99%
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