Redox instability and hemin loss of mutant sperm whale myoglobins induced by 4-hydroxynonenal in vitro

Nantawat Tatiyaborworntham, Cameron Faustman, Shuang Yin, Ranjith Ramanathan, Richard A. Mancini, Surendranath P. Suman, Carol M. Beach, Naveena B. Maheswarappa, Eric W. Grunwald, Mark P. Richards

Research output: Contribution to journalArticlepeer-review

15 Scopus citations

Abstract

The effects of 4-hydroxy-2-nonenal (HNE) on redox stability of Oxy- and Deoxy- wild-type (WT) and recombinant sperm whale myoglobins (P88H/Q152H, L29F, H97A, and H64F) and hemin loss from Met-myoglobin (Mb) were investigated. HNE induced greater redox instability in WT and mutant Mbs compared to controls (p < 0.05). The extent of HNE-induced OxyMb oxidation was lesser in L29F (p < 0.05) and greater in H97A and P88H/Q152H than in WT (p < 0.05). H64F DeoxyMb was more redox stable than WT DeoxyMb in the presence of HNE (p < 0.05). HNE alkylation occurred exclusively on histidine residues, and histidine 48 was alkylated in all sperm whale myoglobins. HNE alkylation accelerated the protoporphyrin moiety loss only in H97A. Met- forms of WT and L29F but not Deoxy- or Oxy- forms released hemin during storage. Primary structure strongly influenced Mb redox stability in the presence of reactive secondary lipid oxidation products.

Original languageEnglish
Pages (from-to)8473-8483
Number of pages11
JournalJournal of Agricultural and Food Chemistry
Volume60
Issue number34
DOIs
StatePublished - Aug 29 2012

Keywords

  • HNE
  • hemin
  • mutant
  • myoglobin
  • redox stability

ASJC Scopus subject areas

  • General Chemistry
  • General Agricultural and Biological Sciences

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