Zhang Yanhong, Hogg Neil
Department of Biophysics and Free Radical Research Center, Medical College of Wisconsin, 8701 Watertown Plank Road, Milwaukee, WI 53226, USA.
Free Radic Biol Med. 2004 Apr 15;36(8):947-58. doi: 10.1016/j.freeradbiomed.2004.01.008.
It has been suggested that S-nitrosohemoglobin (HbSNO) is an oxygen-dependent mediator of nitric oxide delivery to vascular smooth muscle cells, thus regulating vascular tone and blood flow. Central to this much-debated hypothesis is the concept that our previous understanding of the interaction between nitric oxide and ferrous hemoglobin was deficient. In this review we will examine the chemical and biochemical mechanisms for the formation of HbSNO, the properties of HbSNO, and the release of nitric oxide from HbSNO. This review concludes that although novel reactions of nitric oxide, nitrite, and S-nitrosothiols with hemoglobin have been uncovered, there is little evidence to support the notion that the interaction of nitric oxide with ferrous hemoglobin is more complex than had been previously established.
有人提出,S-亚硝基血红蛋白(HbSNO)是一氧化氮向血管平滑肌细胞输送的氧依赖性介质,从而调节血管张力和血流量。这一备受争议的假说的核心概念是,我们之前对一氧化氮与亚铁血红蛋白之间相互作用的理解存在缺陷。在这篇综述中,我们将研究HbSNO形成的化学和生化机制、HbSNO的特性以及一氧化氮从HbSNO中的释放。这篇综述的结论是,尽管已发现一氧化氮、亚硝酸盐和S-亚硝基硫醇与血红蛋白的新反应,但几乎没有证据支持一氧化氮与亚铁血红蛋白的相互作用比之前所确定的更为复杂这一观点。