体外 4-羟壬烯醛诱导的突变抹香鲸肌红蛋白的氧化还原不稳定性和血红素丢失。
Redox instability and hemin loss of mutant sperm whale myoglobins induced by 4-hydroxynonenal in vitro.
机构信息
Department of Animal Science, University of Connecticut , Storrs, Connecticut 06269, United States.
出版信息
J Agric Food Chem. 2012 Aug 29;60(34):8473-83. doi: 10.1021/jf301770p. Epub 2012 Aug 20.
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.
研究了 4-羟基-2-壬烯醛（HNE）对氧合和脱氧野生型（WT）和重组抹香鲸肌红蛋白（P88H/Q152H、L29F、H97A 和 H64F）以及血红素从 Met-肌红蛋白（Mb）中的损失的氧化还原稳定性的影响。与对照组相比，HNE 诱导 WT 和突变 Mb 的氧化还原不稳定性更大（p < 0.05）。与 WT 相比，L29F 中 HNE 诱导的 OxyMb 氧化程度较小（p < 0.05），而 H97A 和 P88H/Q152H 中则较大（p < 0.05）。在 HNE 存在下，H64F 脱氧 Mb 比 WT 脱氧 Mb 具有更高的氧化还原稳定性（p < 0.05）。HNE 烷基化仅发生在组氨酸残基上，并且所有抹香鲸肌红蛋白中的组氨酸 48 都被烷基化。HNE 烷基化仅在 H97A 中加速原卟啉部分的损失。在储存过程中，只有 WT 和 L29F 的 Met-形式，而不是 Deoxy-或 Oxy-形式释放血红素。在存在反应性二级脂质氧化产物的情况下，一级结构强烈影响 Mb 的氧化还原稳定性。
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