Redox instability and hemin loss of mutant sperm whale myoglobins induced by 4-hydroxynonenal in vitro.
Redox instability and hemin loss of mutant sperm whale myoglobins induced by 4-hydroxynonenal in vitro.
复制标题
4-羟基壬烯醛体外诱导突变抹香鲸肌红蛋白的氧化还原不稳定性和血红素损失。
DOI：
10.1021/jf301770p
复制
发表时间：
2012
影响因子：
6.1
通讯作者：
Richards,MarkP
中科院分区：
文献类型：
--
作者：
Tatiyaborworntham,Nantawat;Faustman,Cameron;Yin,Shuang;Ramanathan,Ranjith;Mancini,RichardA;Suman,SurendranathP;Beach,CarolM;Maheswarappa,NaveenaB;Grunwald,EricW;Richards,MarkP
研究了4-羟基-2-壬烯醛（HNE）对氧-和脱氧-野生型（WT）和重组抹香鲸肌红蛋白（P88 H/Q152 H、L29 F、H97 A和H64 F）的氧化还原稳定性以及高铁肌红蛋白（Mb）的氯化血红素损失的影响。与对照相比，HNE在WT和突变型Mb中诱导更大的氧化还原不稳定性（p< 0.05）。HNE诱导的OxyMb氧化的程度在L29 F中比在WT中小（p< 0.05），在H97 A和P88 H/Q152 H中比在WT中大（p< 0.05）。在HNE存在下，H64 F DeoxyMb比WT DeoxyMb更氧化还原稳定（p< 0.05）。HNE烷基化只发生在组氨酸残基上，组氨酸48在所有抹香鲸肌红蛋白中被烷基化。HNE烷基化仅在H97 A中加速原卟啉部分的损失。WT和L29 F的Met-形式在储存期间释放氯化血红素，但不释放脱氧或氧合形式。一级结构强烈影响Mb的氧化还原稳定性的反应性二级脂质氧化产物的存在下。
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.