Reactions between nitrosopersulfide and heme proteins.
Reactions between nitrosopersulfide and heme proteins.
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DOI：
10.1016/j.freeradbiomed.2016.09.005
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发表时间：
2016-10
影响因子：
7.4
通讯作者：
Kim-Shapiro, Daniel B.
中科院分区：
文献类型：
--
作者：
Bolden, Crystal;King, S. Bruce;Kim-Shapiro, Daniel B.
当亚硝基硫醇与过量的硫化氢（H2S）反应时，它们会形成几种中间体，包括亚硝基过硫化物（SSNO−）。这个物种的稳定性和重要性一直存在争议。虽然一些数据表明SSNO -可以是NO活性的相对稳定来源，但另一些数据表明该物种降解得太快了。我们发现这个物种在隔离状态下相对稳定。由于人体中含铁蛋白的丰富和突出，建立含铁蛋白和含铁蛋白与SSNO−的相互作用是很重要的。研究SSNO -与血红素蛋白的反应也可以提供关于该物种体内潜在稳定性和自发反应性的信息。我们利用时间分辨电子顺磁共振和紫外-可见吸收光谱研究了SSNO -与血红素蛋白的反应。当SSNO -与脱氧血红蛋白和脱氧高铁血红蛋白反应时，形成铁亚硝基血红蛋白，表明SSNO -形成NO。然而，与脱氧血红蛋白反应时，亚硝基血红蛋白的产率远低于与脱氧高铁血红蛋白反应时。当SSNO -与羧化血红蛋白、HbCO反应时，很少或不形成亚硝基血红蛋白，而当SSNO -与氧合血红蛋白反应时，很少形成高铁血红蛋白。综上所述，这些数据证实了no的释放，但表明需要一个空血红素来促进血红素-SSNO -直接反应以形成大量no。这些数据还表明，高铁血红蛋白中的铁增强了SSNO -反应性。这些结果可能会影响NO和硫化物的生物利用度和反应性。
When nitrosothiols react with excess hydrogen sulfide, H2S, they form several intermediates including nitrosopersulfide (SSNO−). The stability and importance of this species has been debated. While some data suggest SSNO− can be a relatively stable source of NO activity, others suggest that the species degrades too quickly. We find the species to be relatively stable in isolation. Due to the abundance and prominence of iron-containing proteins throughout the human body, it is important to establish the interaction of ferrous- and ferric-iron containing proteins with SSNO−. Study of the reactions of SSNO− with heme proteins can also provide information about the potential in vivo stability and spontaneous reactivity of this species. We have used time-resolved electron paramagnetic resonance and UV-Vis absorption spectroscopy to study the reactions of SSNO− with heme proteins. Iron-nitrosyl hemoglobin is formed when SSNO− is reacted with deoxyhemoglobin and deoxygenated methemoglobin, suggesting NO formation from SSNO−. However, the yields of nitrosyl hemoglobin in reactions of SSNO− with deoxyhemoglobin are much less than when SSNO− is reacted with deoxygenated methemoglobin. Very little to no nitrosyl hemoglobin is formed when SSNO−is reacted carboxyhemoglobin, HbCO, and when SSNO− is reacted with oxygenated hemoglobin, minimal methemoglobin is formed Taken together, these data confirm the release of NO, but indicate a vacant heme is necessary to facilitate a direct heme-SSNO− reaction to form substantial NO. These data also suggest that the ferric iron in methemoglobin potentiates SSNO− reactivity. These results could potentially impact NO and sulfide bioavailability and reactivity.
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影响因子：
7.4
作者：
Helms, Christine;Kim-Shapiro, Daniel B.
通讯作者：
Kim-Shapiro, Daniel B.
DOI：
10.1161/atvbaha.110.209783
发表时间：
2010-10-01
影响因子：
8.7
作者：
Bucci, Mariarosaria;Papapetropoulos, Andreas;Cirino, Giuseppe
通讯作者：
Cirino, Giuseppe
DOI：
10.1111/j.1432-1033.1995.tb20798.x
发表时间：
1995-08-15
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
BROWN, GC
通讯作者：
BROWN, GC
影响因子：
7.4
作者：
King, S. Bruce
通讯作者：
King, S. Bruce
影响因子：
15
作者：
Hoshino, M;Maeda, M;Ford, PC
通讯作者：
Ford, PC