Formate binding near the redox-active TyrosineD in Photosystem II: consequences on the properties of TyrD View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-06

AUTHORS

Rainer Hienerwadel, Samuel Gourion-Arsiquaud, Matteo Ballottari, Roberto Bassi, Bruce A. Diner, Catherine Berthomieu

ABSTRACT

Formate 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... »

PAGES

139-144

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11120-005-0637-x

DOI

http://dx.doi.org/10.1007/s11120-005-0637-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028766314

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16049766


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52 hydrogen bonding network
53 hydrogen-bonding interactions
54 influence
55 influence of formate
56 interaction
57 latter condition
58 mode
59 model
60 neighbouring
61 network
62 observations
63 oxidation
64 perturbations
65 photosystem II
66 presence
67 presence of formate
68 properties
69 protein
70 proton uptake
71 protonation
72 protons
73 rate
74 recent structural models
75 samples
76 side chains
77 solution
78 spectroscopy
79 stability
80 strong electrostatic interactions
81 structural model
82 tyrosineD
83 uptake
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