Nitric oxide transfer from the NO-donor S-nitroso-N-acetylpenicillamine to monomers and dimers of water-soluble iron-porphyrins

Side-chain-controlled H- and J-aggregation of amphiphilic porphyrins in CTAB micelles

“…It is well accepted that geometries aggregate arrangement of dyes influences their fluorescence characteristics intensively [11,[33][34][35]. According to the exciton theory, the split excitedstate electronic energy levels result from two possible orientations of the transition dipole moments in the excited state while the ground state remains unsplit.…”

A novel pH-controlled transfer process of 5,10,15-tri(4-hydroxyphenyl)-20-(4-hexadecyloxyphenyl) porphyrin in CTAB micelles

“…It has been shown that porphyrins anchored to lipid bilayers and micelles could be applied successfully for reversible binding of dioxygen or nitric oxide in aqueous solutions [1,2]. Incorporation of porphyrins into micelles dramatically influences the aggregation mode and location of these molecules and alters their metallation rate and nitric oxide transfer rate [2][3][4].…”

“…It has been shown that porphyrins anchored to lipid bilayers and micelles could be applied successfully for reversible binding of dioxygen or nitric oxide in aqueous solutions [1,2]. Incorporation of porphyrins into micelles dramatically influences the aggregation mode and location of these molecules and alters their metallation rate and nitric oxide transfer rate [2][3][4]. Generally, it is suggested that hydrophobic porphyrins could penetrate the lipid regions of the membranes and distribute into protein-rich membrane domains [5], while highly polar species were assumed to partition mainly into the aqueous compartments [6].…”

Reductive nitrosylation of water-soluble iron porphyrins by S-nitroso-N-acetylpenicillamine: Rate constants and EPR characterization

“…Recently, we studied the nitrosylation of the two watersoluble iron-porphyrins Fe III (TMPyP) and Fe III (TPPS) by the S-nitrosothiol (thionitrite) SNAP [27]. S-nitrosothiols (RSNO) participate in NO bioregulated processes being important NO donors both in vitro and in vivo [28].…”

“…Its rate of NO delivery is slow in the presence of metal chelators such as EDTA [27,32], with a lifetime greater than 40 h [27]. It was observed, however, that the rate of SNAP decomposition decreases to slightly more than one hour when estimated by the oxymyoglobin assay [32], suggesting that hemes create another pathway for SNAP decomposition.…”