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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45 conditions
46 consequences
47 data
48 electrostatic interactions
49 environment
50 formate
51 formation
52 group
53 hydrogen bonding network
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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