کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10872899 | 1074252 | 2005 | 4 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase
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کلمات کلیدی
EXAFSHDRDTTSSRLcoenzyme MHeterodisulfide reductaseMethanothermobacter marburgensisXAS - HASFourier transform - تبدیل فوریهEPR - تشدید پارامغناطیس الکترونElectron paramagnetic resonance - تشدید پارامغناطیس الکترونdithiothreitol - دیتیوتریتولextended X-ray absorption fine structure - ساختار ریز جذب جذب اشعه ایکسX-ray absorption spectroscopy - طیف سنجی جذب اشعه ایکسIron–sulfur protein - پروتئین آهن گوگرد
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase Direct interaction of coenzyme M with the active-site Fe-S cluster of heterodisulfide reductase](/preview/png/10872899.png)
چکیده انگلیسی
Heterodisulfide reductase (HDR) catalyzes the formation of coenzyme M (CoM-SH) and coenzyme B (CoB-SH) by the reversible reduction of the heterodisulfide, CoM-S-S-CoB. This reaction recycles the two thiol coenzymes involved in the final step of microbial methanogenesis. Electron paramagnetic resonance (EPR) and variable-temperature magnetic circular dichroism spectroscopic experiments on oxidized HDR incubated with CoM-SH revealed a SÂ =Â 1/2 [4Fe-4S]3+ cluster, the EPR spectrum of which is broadened in the presence of CoM-33SH [Duin, E.C., Madadi-Kahkesh, S., Hedderich, R., Clay, M.D. and Johnson, M.K. (2002) Heterodisulfide reductase from Methanothermobacter marburgensis contains an active-site [4Fe-4S] cluster that is directly involved in mediating heterodisulfide reduction. FEBS Lett. 512, 263-268; Duin, E.C., Bauer, C., Jaun, B. and Hedderich, R. (2003) Coenzyme M binds to a [4Fe-4S] cluster in the active site of heterodisulfide reductase as deduced from EPR studies with the [33S]coenzyme M-treated enzyme. FEBS Lett. 538, 81-84]. These results provide indirect evidence that the disulfide binds to the iron-sulfur cluster during reduction. We report here direct structural evidence for this interaction from Se X-ray absorption spectroscopic investigation of HDR treated with the selenium analog of coenzyme M (CoM-SeH). Se K edge extended X-ray absorption fine structure confirms a direct interaction of the Se in CoM-SeH-treated HDR with an Fe atom of the Fe-S cluster at an Fe-Se distance of 2.4Â Ã
.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 579, Issue 7, 14 March 2005, Pages 1741-1744
Journal: FEBS Letters - Volume 579, Issue 7, 14 March 2005, Pages 1741-1744
نویسندگان
Jacob E. Shokes, Evert C. Duin, Carsten Bauer, Bernhard Jaun, Reiner Hedderich, Jürgen Koch, Robert A. Scott,