My Road to Biophysics: Picking Flowers on the Way to Photosynthesis

Fehér, G.

doi:10.1146/annurev.biophys.31.082901.134147

Cited by 12 publications

(5 citation statements)

References 154 publications

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“…High-resolution X-ray crystallographic structures of the photosynthetic complexes are the results of such a successful research on the way to find the relationship between strucmre and function of the involved biological macromolecules. The functional core of the photosynthetic reaction center (RC) is an integral membrane protein complex that is composed of three polypeptide subunits (L, M and H) and ten noncovalently bound cofactors (four bacteriochlorophylls, two bacteriopheophytins, two quinone molecules, a nonheme iron anda carotenoid) [3,4]. This complex with particular spatial configuration plays a central role in the process of energy conversion.…”

Section: Introductionmentioning

confidence: 99%

Spin-labeled photosynthetic reaction centers fromRhodobacter sphaeroides studied by electron paramagnetic resonance spectroscopy and molecular dynamics simulations

et al. 2007

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A new strategy has been applied that combines molecular dynamics (MD) simulations and electron paramagnetic resonance (EPR) spectroscopy to study the structure and conformational dynamics of the spin-labeled photosynthetic reaction center (RC) of Rhodobacter sphaeroides. This protein serves here asa model system to demonstrate the applicability of this new methodology. The RC contains five native cysteines and EPR experiments show that only one cysteine, located on the H subunit, is accessible for spin labeling. The EPR spectra calculated from MD simulation trajectories of spin labels bound to the native cysteines C156 and C234 in subunit H reveal that only the spin label side chain at position 156 provides a spectrum which agrees with the experimental EPR spectrum.

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Section: Introductionmentioning

confidence: 99%

Spin-labeled photosynthetic reaction centers fromRhodobacter sphaeroides studied by electron paramagnetic resonance spectroscopy and molecular dynamics simulations

et al. 2007

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“…George Feher had coined the name ENDOR that evidently stands for “electron–nuclear double resonance”. Interestingly, Feher had been inspired for choosing this acronym also by the Old Testament [ 15 ]: King Saul of the Kingdom of Israel did the unthinkable when menacingly asking the Witch (a magician woman) of Endor (a village south of Mt. Tabor near the Sea of Galilee) to make visible the invisible and to tell him the untellable: What will be his fate next day in the battle against the assembled forces of the Philistines (see The Old Testament, Samuel I, Chapter 28:7).…”

Section: The Early Years Of the Endor Connectionmentioning

confidence: 99%

Jim Hyde and the ENDOR Connection: A Personal Account

2017

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In this minireview, we report on our year-long EPR work, such as electron–nuclear double resonance (ENDOR), pulse electron double resonance (PELDOR) and ELDOR-detected NMR (EDNMR) at X-band and W-band microwave frequencies and magnetic fields. This report is dedicated to James S. Hyde and honors his pioneering contributions to the measurement of spin interactions in large (bio)molecules. From these interactions, detailed information is revealed on structure and dynamics of macromolecules embedded in liquid-solution or solid-state environments. New developments in pulsed microwave and sweepable cryomagnet technology as well as ultra-fast electronics for signal data handling and processing have pushed the limits of EPR spectroscopy and its multi-frequency extensions to new horizons concerning sensitivity of detection, selectivity of molecular interactions and time resolution. Among the most important advances is the upgrading of EPR to high magnetic fields, very much in analogy to what happened in NMR. The ongoing progress in EPR spectroscopy is exemplified by reviewing various multi-frequency electron–nuclear double-resonance experiments on organic radicals, light-generated donor–acceptor radical pairs in photosynthesis, and site-specifically nitroxide spin-labeled bacteriorhodopsin, the light-driven proton pump, as well as EDNMR and ENDOR on nitroxides. Signal and resolution enhancements are particularly spectacular for ENDOR, EDNMR and PELDOR on frozen-solution samples at high Zeeman fields. They provide orientation selection for disordered samples approaching single-crystal resolution at canonical g-tensor orientations—even for molecules with small g-anisotropies. Dramatic improvements of EPR detection sensitivity could be achieved, even for short-lived paramagnetic reaction intermediates. Thus, unique structural and dynamic information is revealed that can hardly be obtained by other analytical techniques. Micromolar concentrations of sample molecules have become sufficient to characterize stable and transient reaction intermediates of complex molecular systems—offering exciting applications for physicists, chemists, biochemists and molecular biologists.

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“…The functional core of the RC is an integral membrane protein complex comprising three subunits (L, M, and H) and ten cofactors, including bacteriochlorophylls (4), bacteriopheophytins (2), quinones (2), a nonheme iron center, and a carotenoid (Feher 2002). This complex catalyzes light-induced charge separation across the membrane, thereby promoting the primary events of photosynthetic energy transduction (Hoff and Deisenhofer 1997).…”

Section: Epr Analysis Of Spin-labeled Membrane Proteinsmentioning

confidence: 99%

Spin labeling EPR

2009

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Site-directed spin labeling in combination with electron paramagnetic resonance spectroscopy has emerged as an efficient tool to elucidate the structure and conformational dynamics of biomolecules under native-like conditions. This article summarizes the basics as well as recent progress of site-directed spin labeling. Continuous wave EPR spectra analyses and pulse EPR techniques are reviewed with special emphasis on applications to the sensory rhodopsin-transducer complex mediating the photophobic response of the halophilic archaeum Natronomonas pharaonis and the photosynthetic reaction center from Rhodobacter sphaeroides R26.

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My Road to Biophysics: Picking Flowers on the Way to Photosynthesis

Cited by 12 publications

References 154 publications

Spin-labeled photosynthetic reaction centers fromRhodobacter sphaeroides studied by electron paramagnetic resonance spectroscopy and molecular dynamics simulations

Spin-labeled photosynthetic reaction centers fromRhodobacter sphaeroides studied by electron paramagnetic resonance spectroscopy and molecular dynamics simulations

Jim Hyde and the ENDOR Connection: A Personal Account

Spin labeling EPR

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