一氧化氮对过氧化氢酶的可逆结合与抑制作用
Reversible binding and inhibition of catalase by nitric oxide.
作者信息
Brown G C
机构信息
Department of Biochemistry, University of Cambridge, England.
出版信息
Eur J Biochem. 1995 Aug 15;232(1):188-91. doi: 10.1111/j.1432-1033.1995.tb20798.x.
Abstract
The interactions between nitric oxide (NO), H2O2, and catalase were investigated. H2O2 did not cause detectable breakdown of NO in the absence of catalase, but did cause NO breakdown in the presence of catalase. Catalase bound NO, and NO rapidly and reversibly inhibited catalase with a Ki of 0.18 microM. The significance of these results for NO cytotoxicity is discussed.
摘要
研究了一氧化氮（NO）、过氧化氢（H₂O₂）和过氧化氢酶之间的相互作用。在没有过氧化氢酶的情况下，H₂O₂不会导致可检测到的NO分解，但在有过氧化氢酶的情况下会导致NO分解。过氧化氢酶结合NO，并且NO以0.18微摩尔的抑制常数（Ki）快速且可逆地抑制过氧化氢酶。讨论了这些结果对NO细胞毒性的意义。
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