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首页> 外文期刊>Biochemistry >Interaction of Hydrogen Peroxide with Ribulose-l,5-bisphosphate Carboxylase/Oxygenase from Rice
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Interaction of Hydrogen Peroxide with Ribulose-l,5-bisphosphate Carboxylase/Oxygenase from Rice

机译：过氧化氢与水稻核糖-1,5-双磷酸羧化酶/加氧酶的相互作用

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摘要

The properties of rice-derived ribulose-l,5-bisphosphate carboxylase/oxygenase(rubisco)in different concentrations of hydrogen peroxide(H_2O_2)solutions have been studied.The results indicate that at low H_2O_2 concentrations(0.2-10 mM),the properties of rubisco(e.g.,carboxylase activities,structure,and susceptibility to heat denaturation)change slightly.However,at higher H_2O_2 concentrations(10-200 mM),rubisco undergoes an unfolding process,including the loss of secondary and tertiary structure,forming extended hydrophobic interface,and leading to cross-links between large subunits.High concentrations of H_2O_2 can also result in an increase in susceptibility of rubisco to heat denaturation.Further pre-treat-ments with or without reductive reagents to rubisco show that the disulfide bonds in rubisco help to protect the enzyme from damage by H_2O_2 as well as other reactive oxygen species.
机译：研究了水稻来源的核糖-1,5-双磷酸核糖羧化酶/加氧酶（rubisco）在不同浓度的过氧化氢（H_2O_2）溶液中的性质。结果表明，在低浓度的H_2O_2（0.2-10 mM）下，该性质Rubisco的变化（例如，羧化酶的活性，结构和对热变性的敏感性）略有变化。但是，在较高的H_2O_2浓度（10-200 mM）下，rubisco经历了一个解折叠过程，包括二级和三级结构的丧失，形成了扩展的疏水性高浓度的H_2O_2还可导致Rubisco对热变性的敏感性增加。在有或没有还原剂的情况下对Rubisco的进一步预处理表明，rubisco中的二硫键帮助保护酶不受H_2O_2和其他活性氧的损害。

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