Brunori Maurizio, Forte Elena, Arese Marzia, Mastronicola Daniela, Giuffrè Alessandro, Sarti Paolo
Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, I-00185 Rome, Italy.
Biochim Biophys Acta. 2006 Sep-Oct;1757(9-10):1144-54. doi: 10.1016/j.bbabio.2006.05.011. Epub 2006 May 13.
Available information on the molecular mechanisms by which nitric oxide (NO) controls the activity of the respiratory enzyme (cytochrome-c-oxidase) is reviewed. We report that, depending on absolute electron flux, NO at physiological concentrations reversibly inhibits cytochrome-c-oxidase by two alternative reaction pathways, yielding either a nitrosyl- or a nitrite-heme a3 derivative. We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase.
本文综述了一氧化氮(NO)调控呼吸酶(细胞色素c氧化酶)活性的分子机制的现有信息。我们报告称,根据绝对电子通量,生理浓度的NO可通过两种不同的反应途径可逆地抑制细胞色素c氧化酶,生成亚硝酰血红素a3衍生物或亚硝酸血红素a3衍生物。我们探讨了一些假设,设想了NO与细胞色素c氧化酶之间反应的生理和/或病理效应。