HOQNO interaction with cytochrome b in succinate:menaquinone oxidoreductase from Bacillus subtilis
作者： Irina A. Smirnova , Cecilia Hägerhäll , Alexandre A. Konstantinov , Lars Hederstedt
DOI: 10.1016/0014-5793(94)01442-4
关键词: Oxidoreductase 、 Quinone oxidoreductase 、 Cytochrome 、 Stereochemistry 、 Biochemistry 、 Heme B 、 Electron Transport Complex II 、 Quinone 、 Chemistry 、 Heme 、 Reductase
摘要: Abstract 2- n -Heptyl4-hydroxyquinoline- N -oxide (HOQNO) inhibits the succinate:quinone oxidoreductase activity of isolated and membrane-bound succinate:menaquinone B. subtilis . The inhibition pattern resembles closely that observed for α-thenoyltrifluoroacetone carboxins in mitochondrial succinate:ubiquinone oxidoreductase: ca. 90% is highly sensitive to HOQNO ( K i 0.2 μM enzyme) whereas rest 10% proves be resistant inhibitor. binding shown perturb absorption spectrum ferrous di-heme cytochrome b both α Soret bands. In addition, inhibitor bring about a negative shift E m low-potential heme It suggested interacts with menasemiquinone site near suppresses MQ .− -to-MQH 2 step quinone reductase reaction but allows partly MQ-to-MQ transition occur; dismutation formed latter MQH may account enzyme insensitive HOQNO.
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