sg:pub.10.1007/s11120-005-0637-x - Springer Nature SciGraph

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

Journal

TITLE

Photosynthesis Research

ISSUE

1-3

VOLUME

Subjects

FOR: Biological Sciences

FOR: Biochemistry And Cell Biology

FOR: Genetics

FOR: Plant Biology

MESH: Amino Acid Sequence

MESH: Formates

MESH: Hydrogen Bonding

MESH: Oxidation-Reduction

MESH: Photosystem Ii Protein Complex

MESH: Protein Binding

MESH: Protein Conformation

MESH: Spectroscopy, Fourier Transform Infrared

MESH: Spinacia Oleracea

MESH: Synechocystis

MESH: Thylakoids

MESH: Tyrosine

Author Affiliations

Laboratoire de Génétique et de Biophysique des Plantes, Case 901, Faculté des Sciences de Luminy, UMR 6191 CNRS-CEA-Université Aix-Marseille II, Av. de Luminy, 13288, Cedex, Marseille, France

CEA/Cadarache, DSV DEVM Laboratoire de Bioénergétique Cellulaire, Bat 156, UMR 6191 CNRS-CEA-Université Aix-Marseille II, 13108, Cedex, Saint Paul-lez-Durance, France

CR & D, Experimental Station, E. I. du Pont de Nemours & Co., 19880-0173, Wilmington, DE, USA

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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20	″	schema:description	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.
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27	″	schema:keywords	Bistris
28	″	″	D oxidation
29	″	″	FTIR spectroscopy
30	″	″	IR bands
31	″	″	IR data
32	″	″	IR modes
33	″	″	Kn
34	″	″	ME
35	″	″	PS II
36	″	″	Tm
37	″	″	TyrD
38	″	″	TyrD.
39	″	″	arginine side chain
40	″	″	band
41	″	″	bonding network
42	″	″	buffer
43	″	″	carboxylate groups
44	″	″	chain
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
85	″	schema:name	Formate binding near the redox-active TyrosineD in Photosystem II: consequences on the properties of TyrD
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Formate binding near the redox-active TyrosineD in Photosystem II: consequences on the properties of TyrD View Full Text

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