Ontology type: schema:ScholarlyArticle
2005-06
AUTHORSRainer Hienerwadel, Samuel Gourion-Arsiquaud, Matteo Ballottari, Roberto Bassi, Bruce A. Diner, Catherine Berthomieu
ABSTRACTFormate and phosphate affect substantially the rate of tyrosine D (TyrD) oxidation and the stability of the radical Tyr\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ _{\rm D}^{\bullet} $$\end{document} in Photosystem II [Hienerwadel R, Boussac A, Breton J and Berthomieu C (1996) Biochemistry 35: 15447–15460]. This observation prompted us to analyze the influence of formate and phosphate on the environment of TyrD using FTIR spectroscopy. The ν (CO) IR mode of Tyr\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ _{\rm D}^{\bullet} $$\end{document} at 1503 cm−1 remains unchanged whatever the buffer used at pH 6 and whether formate is present or not in the sample. Similarly, the main IR mode of reduced TyrD remains at ≈1250 cm−1 in all tested conditions. We thus conclude that formate does not modify the hydrogen-bonded interactions of TyrD and Tyr\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ _{\rm D}^{\bullet} $$\end{document} with neighbouring D2His189 and D2Gln164. In the TyrD-state, an IR mode of formate significantly different from that observed in solution, is detected using 13C-formate, showing that formate forms a strong electrostatic interaction within PS II. The presence of formate affects also IR bands that may be assigned to an arginine side chain. Upon Tyr\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ _{\rm D}^{\bullet} $$\end{document} formation, formate does not protonate but its binding interaction weakens. A proton uptake by Mes or phosphate buffer is detected, which is not observed when BisTris is used as a buffer. In these latter conditions, IR bands characteristic of the protonation of a carboxylate group of the protein are detected instead. The present IR data and the recent structural model of the TyrD environment proposed by Ferreira KN, Iverson TM, Maghlaoui K, Barber J and Iwata S [(2004) Science 303: 1831–1838], suggest that the proton released upon Tyr\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$ _{\rm D}^{\bullet} $$\end{document} formation is shared within a hydrogen bonding network including D2Arg294, and CP47Glu364 and that perturbation of this network by formate – possibly binding near D2Arg294 – substantially affects the properties of TyrD. More... »
PAGES139-144
http://scigraph.springernature.com/pub.10.1007/s11120-005-0637-x
DOIhttp://dx.doi.org/10.1007/s11120-005-0637-x
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1028766314
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/16049766
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54 | ″ | ″ | hydrogen-bonding interactions |
55 | ″ | ″ | influence |
56 | ″ | ″ | influence of formate |
57 | ″ | ″ | interaction |
58 | ″ | ″ | latter condition |
59 | ″ | ″ | mode |
60 | ″ | ″ | model |
61 | ″ | ″ | neighbouring |
62 | ″ | ″ | network |
63 | ″ | ″ | observations |
64 | ″ | ″ | oxidation |
65 | ″ | ″ | perturbations |
66 | ″ | ″ | photosystem II |
67 | ″ | ″ | presence |
68 | ″ | ″ | presence of formate |
69 | ″ | ″ | properties |
70 | ″ | ″ | protein |
71 | ″ | ″ | proton uptake |
72 | ″ | ″ | protonation |
73 | ″ | ″ | protons |
74 | ″ | ″ | rate |
75 | ″ | ″ | recent structural models |
76 | ″ | ″ | samples |
77 | ″ | ″ | side chains |
78 | ″ | ″ | solution |
79 | ″ | ″ | spectroscopy |
80 | ″ | ″ | stability |
81 | ″ | ″ | strong electrostatic interactions |
82 | ″ | ″ | structural model |
83 | ″ | ″ | tyrosineD |
84 | ″ | ″ | uptake |
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