TY - JOUR
T1 - Redox instability and hemin loss of mutant sperm whale myoglobins induced by 4-hydroxynonenal in vitro
AU - Tatiyaborworntham, Nantawat
AU - Faustman, Cameron
AU - Yin, Shuang
AU - Ramanathan, Ranjith
AU - Mancini, Richard A.
AU - Suman, Surendranath P.
AU - Beach, Carol M.
AU - Maheswarappa, Naveena B.
AU - Grunwald, Eric W.
AU - Richards, Mark P.
PY - 2012/8/29
Y1 - 2012/8/29
N2 - 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.
AB - 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.
KW - HNE
KW - hemin
KW - mutant
KW - myoglobin
KW - redox stability
UR - https://www.scopus.com/pages/publications/84865661876
UR - https://www.scopus.com/pages/publications/84865661876#tab=citedBy
U2 - 10.1021/jf301770p
DO - 10.1021/jf301770p
M3 - Article
C2 - 22873347
AN - SCOPUS:84865661876
SN - 0021-8561
VL - 60
SP - 8473
EP - 8483
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 34
ER -