کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10796127 | 1052694 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A four-subunit cytochrome bc1 complex complements the respiratory chain of Thermus thermophilus
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کلمات کلیدی
Stopped flow kineticsndh-2TMPDPSDORFNDH-1IPTGTOFCytochrome bc1Thermus thermophilusamino acid - آمینو اسیدelectron transfer - انتقال الکترونisopropyl β-D-thiogalactopyranoside - ایزوپروپیل β-D-thiogalactopyranosidetime of flight - زمان پروازRespiratory chain - زنجیر تنفسیMass spectrometry - طیف سنجی جرمیAtmospheric pressure - فشار جو، فشار اتمسفرopen reading frame - قاب خواندن بازIonic strength - قدرت یونیMALDI - مالدیcomplex III - پیچیده IIImatrix-assisted laser desorption ionization - یونیزاسیون لیزر جذب ماتریس
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Several components of the respiratory chain of the eubacterium Thermus thermophilus have previously been characterized to various extent, while no conclusive evidence for a cytochrome bc1 complex has been obtained. Here, we show that four consecutive genes encoding cytochrome bc1 subunits are organized in an operon-like structure termed fbcCXFB. The four gene products are identified as genuine subunits of a cytochrome bc1 complex isolated from membranes of T. thermophilus. While both the cytochrome b and the FeS subunit show typical features of canonical subunits of this respiratory complex, a further membrane-integral component (FbcX) of so far unknown function copurifies as a subunit of this complex. The cytochrome c1 carries an extensive N-terminal hydrophilic domain, followed by a hydrophobic, presumably membrane-embedded helical region and a typical heme c binding domain. This latter sequence has been expressed in Escherichia coli, and in vitro shown to be a kinetically competent electron donor to cytochrome c552, mediating electron transfer to the ba3 oxidase. Identification of this cytochrome bc1 complex bridges the gap between the previously reported NADH oxidation activities and terminal oxidases, thus, defining all components of a minimal, mitochondrial-type electron transfer chain in this evolutionary ancient thermophile.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1708, Issue 2, 30 June 2005, Pages 262-274
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1708, Issue 2, 30 June 2005, Pages 262-274
نویسندگان
Daniela Mooser, Oliver Maneg, Carsten Corvey, Thomas Steiner, Francesco Malatesta, Michael Karas, Tewfik Soulimane, Bernd Ludwig,