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Soluble meso and deuteroporphyrin analogs of the malaria pigment hematin anhydride.
Suárez, Liliana; Kosar, Aaron J; Dodd, Erin L; Tazoo, Dagobert; Lambert, Ambre Charlotte; Bohle, D Scott.
Afiliación
  • Suárez L; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal H3A 0B8, Canada.
  • Kosar AJ; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal H3A 0B8, Canada.
  • Dodd EL; Département de Chimie de l'UQAM, 2101, rue Jeanne-Mance, Montréal H2X 2J6, Canada.
  • Tazoo D; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal H3A 0B8, Canada.
  • Lambert AC; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal H3A 0B8, Canada.
  • Bohle DS; Department of Chemistry, McGill University, 801 Sherbrooke St. W., Montreal H3A 0B8, Canada. Electronic address: scott.bohle@mcgill.ca.
J Inorg Biochem ; 252: 112470, 2024 03.
Article en En | MEDLINE | ID: mdl-38218137
ABSTRACT
Two soluble heme analogs of the insoluble malaria pigment hematin anhydride (HA, or ß-hematin), [Fe(III)(protoporphyrin)]2, with either mesoporphyrin (MHA) or deuteroporphyrin (DHA) are characterized by elemental analysis, SEM, IR spectroscopy, electronic spectroscopy, paramagnetic 1H NMR spectroscopy and solution magnetic susceptibility. While prior single crystal and X-ray powder diffraction results indicate all three have a common propionate linked dimer motif, there is considerable solid state variation in the conformation. This is associated with enhanced solubility of MHA and DHA. As with HA, DHA undergoes thermally promoted reversible hydration/dehydration in the solid state. Solution 1H NMR studies of DHA suggest a high spin dimeric structure with the porphyrin methyls distributed between two isomers which are also present in the solid state. These soluble iron(III)porphyrin dimers allow for the first direct solution studies by NMR and UV-Vis spectroscopies of these key species. Taken together the results illustrate the importance and utility of varying the substituents on the periphery of the porphyrin for studying heme aggregation and malaria pigment formation.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Porfirinas / Hemoproteínas / Hemina Idioma: En Revista: J Inorg Biochem Año: 2024 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Porfirinas / Hemoproteínas / Hemina Idioma: En Revista: J Inorg Biochem Año: 2024 Tipo del documento: Article País de afiliación: Canadá Pais de publicación: Estados Unidos