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H2S and NO cooperatively regulate vascular tone by activating a neuroendocrine HNO–TRPA1–CGRP signalling pathway
Nitroxyl (HNO) is a redox sibling of nitric oxide (NO) that targets distinct signalling pathways with pharmacological endpoints of high significance in the treatment of heart failure. Beneficial HNOExpand
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Heme protein oxygen affinity regulation exerted by proximal effects.
Heme proteins are found in all living organisms and are capable of performing a wide variety of tasks, requiring in many cases the binding of diatomic ligands, namely, O(2), CO, and/or NO. Therefore,Expand
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Nitric oxide interaction with cytochrome c' and its relevance to guanylate cyclase. Why does the iron histidine bond break?
Soluble guanylate cyclase (sGC), the mammalian receptor for nitric oxide (NO), is a heme protein with a histidine as the proximal ligand. Formation of a five-coordinate heme-NO complex with theExpand
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Photodynamic ultradeformable liposomes: Design and characterization.
Hydrophobic ([tetrakis(2,4-dimetil-3-pentyloxi)-phthalocyaninate]zinc(II)) (ZnPc) and hydrophilic ([tetrakis(N,N,N-trimethylammoniumetoxi)-phthalocyaninate]zinc(II) tetraiodide) (ZnPcMet)Expand
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DFT study on the reactivity of iron porphyrins tuned by ring substitution.
The effect of beta-substituents (-NO2, -Br, -OCH3) in the reactivity of Fe(II) and Fe(III) porphyrins is studied by means of density functional theory (DFT) calculations. The binding of nitric oxide,Expand
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Discrimination of nitroxyl and nitric oxide by water-soluble Mn(III) porphyrins.
The water-soluble manganese(III) meso-tetrakis (N-ethylpyridinium-2-yl) porphyrin (Mn(III)TEPyP) and manganese(III) meso-(tetrakis(4-sulfonato-phenyl)) porphyrinate (Mn(III)TPPS) are able toExpand
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A microscopic study of the deoxyhemoglobin-catalyzed generation of nitric oxide from nitrite anion.
There is recent evidence suggesting that nitrite anion (NO 2 (-)) represents the major intravascular NO storage molecule whose transduction to NO is facilitated by a reduction mechanism catalyzed byExpand
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Molecular basis for the electric field modulation of cytochrome C structure and function.
Cytochrome c (Cyt) is a small soluble heme protein with a hexacoordinated heme and functions as an electron shuttle in the mitochondria and in early events of apoptosis when released to theExpand
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Discussing endogenous NO(•)/HNO interconversion aided by phenolic drugs and vitamins.
The reduction of NO(•) to HNO/NO(-) under biologically compatible conditions has always been thought as unlikely, mostly because of the negative reduction potential: E°(NO(•),H(+)/HNO) = -0.55 V vsExpand
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