کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8298541 | 1537031 | 2018 | 21 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Changing the site energy of per-614 in the Peridinin-chlorophyll a-protein does not alter its capability of chlorophyll triplet quenching
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کلمات کلیدی
carotenoid(s)T-Striplet-triplet energy transferTTETODMRENDORZFSChlPCPElectron paramagnetic resonance - تشدید پارامغناطیس الکترونEPR - تشدید پارامغناطیس الکترونZero Field Splitting - تقسیم فیلد صفرper - در هرTriplet state - دولت سه گانهElectron nuclear double resonance - رزونانس دو هسته ای الکترونOptically detected magnetic resonance - رزونانس مغناطیسی تشخیص نوریChlorophyll - سبزینه یا کلروفیلCAR - ماشینPulse EPR - پالس EPRPeridinin - پریدنینCarotenoid - کاروتنوئید
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Changing the site energy of per-614 in the Peridinin-chlorophyll a-protein does not alter its capability of chlorophyll triplet quenching Changing the site energy of per-614 in the Peridinin-chlorophyll a-protein does not alter its capability of chlorophyll triplet quenching](/preview/png/8298541.png)
چکیده انگلیسی
The peridinin-chlorophyll-a protein (PCP) is a water-soluble light harvesting protein of the dinoflagellate Amphidinium carterae, employing peridinin (Per) as the main carotenoid to fulfil light harvesting and photo-protective functions. Per molecules bound to the protein experience specific molecular surroundings which lead to different electronic and spectral properties. In the refolded N89â¯L variant PCP (N89â¯L-RFPCP) a significant part of the intensity on the long wavelength side of the absorption spectrum is shifted to shorter wavelengths due to a significant change in the Per-614 site energy. Since Per-614 has been shown to be the main chlorophyll (Chl) triplet quencher in the protein, and the relative geometry of pigments is not affected by the mutation as verified by X-ray crystallography, this variant is ideally suited to study the dependence of the triplet-triplet energy transfer (TTET) mechanism on the pigment site energy. By using a combination of Optically Detected Magnetic Resonance (ODMR), pulse Electron Paramagnetic Resonance (EPR) and Electron Nuclear DOuble Resonance (ENDOR) we found that PCP maintains the efficient Per-614-to-Chl-a TTET despite the change of Per-614 local energy. This shows the robustness of the photoprotective site, which is very important for the protection of the system.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1859, Issue 8, August 2018, Pages 612-618
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1859, Issue 8, August 2018, Pages 612-618
نویسندگان
Alessandro Agostini, Jens Niklas, Tim Schulte, Marilena Di Valentin, Marco Bortolus, Eckhard Hofmann, Wolfgang Lubitz, Donatella Carbonera,