کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10537249 | 962704 | 2013 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or boâ²' to inhibition by the carbon monoxide-releasing molecule, CORM-3
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کلمات کلیدی
HO-1Respiratory oxidaseCO-RMHaem oxygenase-1CORM-3CORM-2VmaxDCFH-DANACEGTAPBSN-acetylcysteine - N-استیل سیستئینROS - ROSEDTA - اتیلن دی آمین تترا استیک اسید ethylene diamine tetraacetic acid - اتیلن دیامین تتراستیک اسیدethylene glycol tetraacetic acid - اتیلن گلیکول تتراستیک اسیدKLA - ارتش آزادیبخشEscherichia coli - اشریشیا کُلیDissociation constant - حد تفکیکSOD - سدSuperoxide dismutase - سوکسوکس دیسموتازcytochrome - سیتوکرومinductively coupled plasma mass spectrometry - طیفسنجی جرمی پلاسمای جفتشده القاییICP-MS - طیفسنجی جرمی پلاسمای جفتشده القاییLuria Bertani broth - لوریا برتانی برودPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریCarbon monoxide-releasing molecule - مولکول آزاد کننده مونوکسید کربنReactive oxygen species - گونههای فعال اکسیژن
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or boâ²' to inhibition by the carbon monoxide-releasing molecule, CORM-3 Cytochrome bd-I in Escherichia coli is less sensitive than cytochromes bd-II or boâ²' to inhibition by the carbon monoxide-releasing molecule, CORM-3](/preview/png/10537249.png)
چکیده انگلیسی
Background: CO-releasing molecules (CO-RMs) are potential therapeutic agents, able to deliver CO - a critical gasotransmitter - in biological environments. CO-RMs are also effective antimicrobial agents; although the mechanisms of action are poorly defined, haem-containing terminal oxidases are primary targets. Nevertheless, it is clear from several studies that the effects of CO-RMs on biological systems are frequently not adequately explained by the release of CO: CO-RMs are generally more potent inhibitors than is CO gas and other effects of the molecules are evident. Methods: Because sensitivity to CO-RMs cannot be predicted by sensitivity to CO gas, we assess the differential susceptibilities of strains, each expressing only one of the three terminal oxidases of E. coli - cytochrome bd-I, cytochrome bd-II and cytochrome boâ², to inhibition by CORM-3. We present the first sensitive measurement of the oxygen affinity of cytochrome bd-II (Km 0.24 μM) employing globin deoxygenation. Finally, we investigate the way(s) in which thiol compounds abolish the inhibitory effects of CORM-2 and CORM-3 on respiration, growth and viability, a phenomenon that is well documented, but poorly understood. Results: We show that a strain expressing cytochrome bd-I as the sole oxidase is least susceptible to inhibition by CORM-3 in its growth and respiration of both intact cells and membranes. Growth studies show that cytochrome bd-II has similar CORM-3 sensitivity to cytochrome boâ². Cytochromes boâ² and bd-II also have considerably lower affinities for oxygen than bd-I. We show that the ability of N-acetylcysteine to abrogate the toxic effects of CO-RMs is not attributable to its antioxidant effects, or prevention of CO targeting to the oxidases, but may be largely due to the inhibition of CO-RM uptake by bacterial cells. Conclusions: A strain expressing cytochrome bd-I as the sole terminal oxidase is least susceptible to inhibition by CORM-3. N-acetylcysteine is a potent inhibitor of CO-RM uptake by E. coli. General significance: Rational design and exploitation of CO-RMs require a fundamental understanding of their activity. CO and CO-RMs have multifaceted effects on mammalian and microbial cells; here we show that the quinol oxidases of E. coli are differentially sensitive to CORM-3. This article is part of a Special Issue entitled: Oxygen Binding and Sensing Proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1834, Issue 9, September 2013, Pages 1693-1703
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1834, Issue 9, September 2013, Pages 1693-1703
نویسندگان
Helen E. Jesse, Tacita L. Nye, Samantha McLean, Jeffrey Green, Brian E. Mann, Robert K. Poole,