کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1943104 1052646 2009 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Solid-state NMR and functional studies on proteorhodopsin
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Solid-state NMR and functional studies on proteorhodopsin
چکیده انگلیسی

Proteins of the proteorhodopsin (PR) family are found abundantly in many marine bacteria in the photic zone of the oceans. They are colour-tuned to their environment. The green absorbing species has been shown to act as a light-driven proton pump and thus could form a potential source of energy. The pKa of the primary proton acceptor is close to the pH of seawater which could also indicate a regulatory role. Here, we review and summarize our own recent findings in the context of known data and present some new results. Proton transfer in vitro by PR is shown by a fluorescence assay which confirms a pH dependent vectoriality. Previously reported low diffracting 2D crystal preparations of PR are assessed for their use for solid-state NMR by two dimensional 13C–13C DARR spectra. 15N–1H HETCOR MAS NMR experiments show bound water in the vicinity of the protonated Schiff base which could play a role in proton transfer. The effect of highly conserved H75 onto the properties of the chromophore has been investigated by single site mutations. They do show a pronounced effect onto the optical absorption maximum and the pKa of the proton acceptor but have only a small effect onto the 15N chemical shifts of the protonated Schiff base.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Bioenergetics - Volume 1787, Issue 6, June 2009, Pages 697–705
نویسندگان
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