کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8267434 | 1534944 | 2016 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Reactions between nitrosopersulfide and heme proteins
ترجمه فارسی عنوان
واکنش های بین نیتروسپورسولفید و پروتئین هم
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
سولفید هیدروژن، اکسید نیتریک، نیتروکسیل، نیتروسپورسولفید، نیتروستیول،
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
سالمندی
چکیده انگلیسی
When nitrosothiols react with excess hydrogen sulfide, H2S, they form several intermediates including nitrosopersulfide (SSNOâ). The stability and importance of this species has been debated. While some data suggest SSNOâ 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 SSNOâ 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 SSNOâ with heme proteins. Iron-nitrosyl hemoglobin is formed when SSNOâ is reacted with deoxyhemoglobin and deoxygenated methemoglobin, suggesting NO formation from SSNOâ. However, the yields of nitrosyl hemoglobin in reactions of SSNOâ with deoxyhemoglobin are much less than when SSNOâ is reacted with deoxygenated methemoglobin. Very little to no nitrosyl hemoglobin is formed when SSNOâ is reacted carboxyhemoglobin, HbCO, and when SSNOâ 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-SSNOâ 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Free Radical Biology and Medicine - Volume 99, October 2016, Pages 418-425
Journal: Free Radical Biology and Medicine - Volume 99, October 2016, Pages 418-425
نویسندگان
Crystal Bolden, S. Bruce King, Daniel B. Kim-Shapiro,