ODMR spectroscopy of molecular functions in photosynthetic membrane proteins

For the last twenty years, in our laboratory in Padova, we have been studying photosynthetic membrane proteins by optically detected magnetic resonance (ODMR), a spectroscopic tool very suitable to detect characteristics and features of the pigments in their triplet state. These studies parallel the epochal development of membrane protein single-crystal X-ray analysis, started in 1984, of which George Feher was a pioneer. Structural knowledge was a new starting point in asking the proper questions related to the functioning of reaction centers and light-harvesting complex proteins, unique to photosynthesis, and spectroscopists of all kinds found new enlightenment in their searches for function details. The first part of this review will be devoted to describe the molecular species which may be observed by ODMR and explain its principle and why it is a useful and powerful technique in the study of photosynthetic proteins. The second part will illustrate some examples of the functional mechanisms which can be revealed, especially in cases where one is able to look at systems which are among the more complex of those whose structures have been studied. We mean integrated systems where both the reaction centers and the light-harvesting complexes are present in their natural and mutual relationship within the large physiological membrane.

[1]  S. Santabarbara,et al.  A Fluorescence Detected Magnetic Resonance Investigation of the Carotenoid Triplet States Associated with Photosystem II of Isolated Spinach Thylakoid Membranes , 2005, Photosynthesis Research.

[2]  T. Morosinotto,et al.  Quenching of chlorophyll triplet states by carotenoids in reconstituted Lhca4 subunit of peripheral light-harvesting complex of photosystem I. , 2005, Biochemistry.

[3]  W. Saenger,et al.  Theory of optical spectra of photosystem II reaction centers: location of the triplet state and the identity of the primary electron donor. , 2005, Biophysical journal.

[4]  S. Santabarbara,et al.  Carotenoid triplet states associated with the long-wavelength-emitting chlorophyll forms of photosystem I in isolated thylakoid membranes. , 2005, The journal of physical chemistry. B.

[5]  T. Morosinotto,et al.  The Nature of a Chlorophyll Ligand in Lhca Proteins Determines the Far Red Fluorescence Emission Typical of Photosystem I* , 2003, Journal of Biological Chemistry.

[6]  S. Santabarbara,et al.  Analysis of photosystem II triplet states in thylakoids by fluorescence detected magnetic resonance in relation to the redox state of the primary quinone acceptor QA , 2003 .

[7]  S. Santabarbara,et al.  Chlorophyll triplet states associated with photosystem II of thylakoids. , 2002, Biochemistry.

[8]  A. Holzwarth,et al.  Primary Processes and Structure of the Photosystem II Reaction Center: A Photon Echo Study†,‡ , 2000 .

[9]  T. Tomo,et al.  Fourier transform infrared study of the cation radical of P680 in the photosystem II reaction center: evidence for charge delocalization on the chlorophyll dimer. , 1998, Biochemistry.

[10]  D. Carbonera,et al.  The P700 triplet state in an intact environment detected by ODMR A well resolved triplet minus singlet spectrum , 1997 .

[11]  G. Giacometti,et al.  A TIME-RESOLVED ELECTRON NUCLEAR DOUBLE RESONANCE STUDY OF THE PHOTOEXCITED TRIPLET STATE OF P680 IN ISOLATED REACTION CENTERS OF PHOTOSYSTEM II , 1996 .

[12]  D. Carbonera,et al.  A well resolved ODMR triplet minus singlet spectrum of P680 from PSII particles , 1994, FEBS letters.

[13]  G. Searle,et al.  Fluorescence detected magnetic resonance of the primary donor and inner core antenna chlorophyll in Photosystem I reaction centre protein: Sign inversion and energy transfer , 1992, Photosynthesis Research.

[14]  R. V. D. Vos,et al.  Microwave and optical spectroscopy of carotenoid triplets in light-harvesting complex LHC II of spinach by absorbance-detected magnetic resonance , 1991 .

[15]  D. Budil,et al.  The chlorophyll triplet state as a probe of structure and function in photosynthesis. , 1991, Biochimica et biophysica acta.

[16]  M. Mimuro,et al.  Carotenoids in photosynthesis: absorption, transfer and dissipation of light energy , 1991 .

[17]  A. Rutherford,et al.  The influence of the quinone-iron electron acceptor complex on the reaction centre photochemistry of Photosystem II , 1989 .

[18]  G. Feher,et al.  Structure and function of bacterial photosynthetic reaction centres , 1989, Nature.

[19]  T O Yeates,et al.  Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[20]  J Deisenhofer,et al.  X-ray structure analysis of a membrane protein complex. Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. , 1984, Journal of molecular biology.

[21]  A. Jongenelis,et al.  High‐resolution triplet‐minus‐singlet absorbance difference spectrum of photosystem II particles , 1983 .

[22]  P. Bolton Triplet state ODMR spectroscopy : edited by Richard H. Clarke, John Wiley and Sons 1982. £43.75 (x + 566 pages) ISBN 0 471 07988 X , 1983 .

[23]  E. Schlodder,et al.  Modeling of Optical Spectra and Light Harvesting in Photosystem I , 2006 .

[24]  G. Feher Three decades of research in bacterial photosynthesis and the road leading to it: A personal account , 2004, Photosynthesis Research.

[25]  C. Vannini,et al.  Fluorescence and absorption detected magnetic resonance of chlorosomes from green bacteria Chlorobium tepidum and Chloroflexus aurantiacus. A comparative study , 2001 .