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氧化还原化合物对NAD(P)H:FMN氧化还原酶-荧光素酶生物发光系统的影响。

Redox compounds influence on the NAD(P)H:FMN-oxidoreductase-luciferase bioluminescent system.

作者信息

Vetrova E V, Kudryasheva N S, Kratasyuk V A

机构信息

Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russia.

出版信息

Photochem Photobiol Sci. 2007 Jan;6(1):35-40. doi: 10.1039/b608152e. Epub 2006 Dec 11.

Abstract

A review of the mechanisms of the exogenous redox compounds influence on the bacterial coupled enzyme system: NAD(P)H:FMN-oxidoreductase-luciferase has been done. A series of quinones has been used as model organic oxidants. The three mechanisms of the quinones' effects on bioluminescence were suggested: (1) inhibition of the NADH-dependent redox reactions; (2) interactions between the compounds and the enzymes of the coupled enzyme system; and (3) intermolecular energy migration. The correlation between the kinetic parameters of bioluminescence and the standard redox potential of the quinones proved that the inhibition of redox reactions was the key mechanism by which the quinones decrease the light emission intensity. The changes in the fluorescence anisotropy decay of the endogenous flavin of the enzyme preparations showed the direct interaction between quinones and enzymes. It has been demonstrated that the intermolecular energy migration mechanism played a minor role in the effect of quinones on the bioluminescence. A comparative analysis of the effect of quinones, phenols and inorganic redox compounds on bioluminescent coupled enzyme systems has been carried out.

摘要

对外源氧化还原化合物对细菌偶联酶系统

NAD(P)H:FMN-氧化还原酶-荧光素酶的影响机制进行了综述。一系列醌类被用作模型有机氧化剂。提出了醌类对生物发光影响的三种机制:(1)抑制NADH依赖的氧化还原反应;(2)化合物与偶联酶系统的酶之间的相互作用;(3)分子间能量迁移。生物发光动力学参数与醌类标准氧化还原电位之间的相关性证明,氧化还原反应的抑制是醌类降低发光强度的关键机制。酶制剂内源性黄素荧光各向异性衰减的变化表明醌类与酶之间存在直接相互作用。已证明分子间能量迁移机制在醌类对生物发光的影响中起次要作用。对醌类、酚类和无机氧化还原化合物对生物发光偶联酶系统的影响进行了比较分析。

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