کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10872678 | 1074212 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Thermodynamic and EPR studies of slowly relaxing ubisemiquinone species in the isolated bovine heart complex I
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کلمات کلیدی
ubiquinoneFMNubisemiquinoneSuccinate-ubiquinone oxidoreductaseUbiquinol-cytochrome c oxidoreductaseNADH-Ubiquinone oxidoreductaseNADH:ubiquinone oxidoreductase - NADH: ubiquinone oxidoreductaseΔμH+ - ΔHH +EPR - تشدید پارامغناطیس الکترونElectron paramagnetic resonance - تشدید پارامغناطیس الکترونSMP - دانشکده دبیرستانelectrochemical proton gradient - شیب پروتون الکتروشیمیاییEPR spectrum - طیف EPRflavin mononucleotide - فلاون مونونوکلئوتیدComplex I - مجتمع IComplex II - مجتمع دومmidpoint redox potential - پودر reddo midpointcomplex III - پیچیده III
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Previously, we investigated ubisemiquinone (SQ) EPR spectra associated with NADH-ubiquinone oxidoreductase (complex I) in the tightly coupled bovine heart submitochondrial particles (SMP). Based upon their widely differing spin relaxation rate, we distinguished SQ spectra arising from three distinct SQ species, namely SQNf (fast), SQNs (slow), and SQNx (very slow). The SQNf signal was observed only in the presence of the proton electrochemical gradient (ÎμH+), while SQNs and SQNx species did not require the presence of ÎμH+. We have now succeeded in characterizing the redox and EPR properties of SQ species in the isolated bovine heart complex I. The potentiometric redox titration of the gz,y,x = 2.00 semiquinone signal gave the redox midpoint potential (Em) at pH 7.8 for the first electron transfer step [Em1(Q/SQ)] of â45 mV and the second step [Em2(SQ/QH2)] of â63 mV. It can also be expressed as [Em(Q/QH2)] of â54 mV for the overall two electron transfer with a stability constant (Kstab) of the SQ form as 2.0. These characteristics revealed the existence of a thermodynamically stable intermediate redox state, which allows this protein-associated quinone to function as a converter between n = 1 and n = 2 electron transfer steps. The EPR spectrum of the SQ species in complex I exhibits a Gaussian-type spectrum with the peak-to-peak line width of â¼6.1 G at the sample temperature of 173 K. This indicates that the SQ species is in an anionic Qâ state in the physiological pH range. The spin relaxation rate of the SQ species in isolated complex I is much slower than the SQ counterparts in the complex I in situ in SMP. We tentatively assigned slow relaxing anionic SQ species as SQNs, based on the monophasic power saturation profile and several fold increase of its spin relaxation rate in the presence of reduced cluster N2. The current study also suggests that the very slowly relaxing SQNx species may not be an intrinsic complex I component. The functional role of SQNs is further discussed in connection with the SQNf species defined in SMP in situ.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 579, Issue 2, 17 January 2005, Pages 500-506
Journal: FEBS Letters - Volume 579, Issue 2, 17 January 2005, Pages 500-506
نویسندگان
Tomoko Ohnishi, Jerry E. Jr., Takahiro Yano, Russell LoBrutto, William R. Widger,