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The reactions of hydropersulfides (RSSH) with myoglobin.
Álvarez, Lucía; Suarez Vega, Valeria; McGinity, Christopher; Khodade, Vinayak S; Toscano, John P; Nagy, Peter; Lin, Joseph; Works, Carmen; Fukuto, Jon M.
Afiliação
  • Álvarez L; Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, INQUIMAE-CONICET, Ciudad Universitaria, (C1428EGA) Buenos Aires, Argentina.
  • Suarez Vega V; Department of Chemistry, Sonoma State University, Rohnert Park, CA, 94928, USA.
  • McGinity C; Department of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA.
  • Khodade VS; Department of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA.
  • Toscano JP; Department of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA.
  • Nagy P; Department of Molecular Immunology and Toxicology, National Institute of Oncology, Budapest, Hungary.
  • Lin J; Department of Biology, Sonoma State University, Rohnert Park, CA, 94928, USA.
  • Works C; Department of Chemistry, Sonoma State University, Rohnert Park, CA, 94928, USA.
  • Fukuto JM; Department of Chemistry, Sonoma State University, Rohnert Park, CA, 94928, USA; Department of Chemistry, Johns Hopkins University, Baltimore, MD, 21218, USA. Electronic address: fukuto@sonoma.edu.
Arch Biochem Biophys ; 687: 108391, 2020 07 15.
Article em En | MEDLINE | ID: mdl-32360749
Hydropersulfides are reported to be good biological reductants, superior to thiols and akin to selenols. As such, they have been previously shown to reduce metalloproteins such as ferric myoglobin and ferric cytochrome c to their ferrous forms under conditions where little or no reduction from corresponding thiols is observed. Not surprisingly, the reduction of ferric myoglobin to ferrous myoglobin under aerobic conditions results in the generation of oxymyoglobin (dioxygen bound ferrous myoglobin). Previous studies have demonstrated that oxymyoglobin can also act as an oxidant with highly reducing species such as hydroxylamine and ascorbate. Considering the reducing properties of hydropersulfides, it is possible that they can also react with oxymyoglobin similarly to hydroxylamine or ascorbate. Herein, this reaction is examined and indeed hydropersulfides are found to react with oxymyoglobin similarly to other reducing species leading to a fleeting ferric myoglobin which is rapidly reduced to the ferrous form also by hydropersulfide.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Sulfetos / Mioglobina Limite: Animals Idioma: En Revista: Arch Biochem Biophys Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Sulfetos / Mioglobina Limite: Animals Idioma: En Revista: Arch Biochem Biophys Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Argentina País de publicação: Estados Unidos