Spectroscopic studies of water-soluble superstructured iron(III) porphyrin. Interaction with the bovine serum albumin protein

• Published in: Journal of coordination chemistry Vol. 71; no. 6; pp. 890 - 905
• Main Authors: Jiménez, Hermas R., Arbona, María
• Format: Journal Article
• Language: English
• Published: Abingdon Taylor & Francis Ltd 19-03-2018
• Subjects: Electron paramagnetic resonance; Electronic structure; Iron; NMR; Nuclear magnetic resonance; Proteins; Serum albumin; Temperature dependence; Titration
• ISSN: 0095-8972; 1029-0389
• DOI: 10.1080/00958972.2018.1434624

Acid-base equilibrium of the "one-face"-hindered sulfonated porphyrin, α5,15-[2,2[vprime](dodecamethyleneoxy),(5-sulfonato)diphenyl]-10,20-bis(2-hydroxy,5-sulfonatophenyl)porphyrinato iron(III), has been studied by paramagnetic 1H NMR. The isotropically shifted signals change in a fast exchange regime on the NMR time-scale. 1H longitudinal relaxation times and temperature dependence of the chemical shifts were measured and analyzed. The electronic structure of hydroxo specie is characteristic of a six- or five-coordinate high-spin iron(III) porphyrin with an S = 5/2 ground state. The 1H NMR titration allowed determination of the acidity constant, pKa 6.2 (0.1 M KNO3, 25 °C). In addition, we also report the interaction between the monohydroxo iron(III) porphyrin and the bovine serum albumin protein. From a 1H NMR titration, we have determined the affinity apparent constant, log Kap 3.2 (pH 7, KNO3 0.1 M, 25 °C). The formation of superstructured iron porphyrin-albumin protein adduct was confirmed by electronic absorption spectroscopy and electron paramagnetic resonance.