Search Results - "Hoff, A.J"

Photophysics of photosynthesis. Structure and spectroscopy of reaction centers of purple bacteria by Hoff, A.J., Deisenhofer, J.

“…The fundamental photochemical reaction of photosynthetic energy conversion, which transforms the photon energy of light in chemical free energy, takes places…”
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Selective excitation in pulsed EPR of spin-correlated radical pairs: electron–electron interactions, zero-, single-, and double-quantum relaxation and spectral diffusion by Borovykh, I.V., Kulik, L.V., Dzuba, S.A., Hoff, A.J.

“…Experiments are described in which a low-amplitude microwave pulse excites only one out of four allowed transitions of a spin-correlated radical pair (SCRP). A…”
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Interactions between chromophores in reaction centers of purple bacteria. A reinterpretation of the triplet-minus-singlet spectra of Rhodobacter sphaeroides R26 and Rhodopseudomonas viridis by Vrieze, J., Hoff, A.J.

“…The orientations of the optical transition moments contributing to the Q Y-region of the triplet-minus-singlet absorbance-difference spectrum of the reaction…”
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Effect of bicarbonate on the S2 multiline EPR signal of the oxygen‐evolving complex in photosystem II membrane fragments by Hulsebosch, R.J, Allakhverdiev, S.I, Klimov, V.V, Picorel, R, Hoff, A.J

“…Removal of bicarbonate from spinach photosystem II BBY particles by means of washing in a CO2‐free medium results in the loss of their capability to accumulate…”
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Electron paramagnetic resonance of the primary radical pair [D ·+φA·−] in reaction centers of photosynthetic bacteria by Proskuryakov, I.I., Klenina, I.B., Hore, P.J., Bosch, M.K., Gast, P., Hoff, A.J.

“…Using continuous wave EPR spectroscopy with a high time resolution, a new short-lived signal at g = 2 is observed in bacterial photosynthetic reaction centers…”
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The triplet state of the FMO complex of the green sulfur bacterium Prosthecochloris aestuarii studied with single-crystal EPR by Louwe, R.J.W., Aartsma, T.J., Gast, P., Hulsebosch, R.J., Nan, H.M., Vrieze, J., Hoff, A.J.

“…Triplet-electron paramagnetic resonance (EPR) spectra were obtained of single crystals of the FMO complex of the green sulfur bacterium Prostecochloris…”
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Jan Amesz by Hoff, A.J, Aartsma, T.J

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Electron spin echo studies on chloroplasts. Spectral characteristics of electron transport components and light-induced transients by Nishi, N, Hoff, A J, van der Waals, J H

“…Electron-spin resonance echoes are used to study the complex overlapping ESR spectra of whole chloroplasts. By varying the repetition rate of the microwave…”
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Oscillations within the BL absorption band of Rhodobacter sphaeroides reaction centers upon 30 femtosecond excitation at 865 nm by Streltsov, A.M., Aartsma, T.J., Hoff, A.J., Shuvalov, V.A.

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Probing the energy landscape of bacterial photosynthetic reaction centers at cryogenic temperatures by ESEEM of spin-polarised D +Q A− radical pairs by Dzuba, S.A., Gast, P., Hoff, A.J.

“…The energy landscape of the reaction center protein of the photosynthetic bacterium Rhodobacter sphaeroides R-26 has been investigated with electron spin echo…”
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Oscillations within the B L absorption band of Rhodobacter sphaeroides reaction centers upon 30 femtosecond excitation at 865 nm by Streltsov, A.M., Aartsma, T.J., Hoff, A.J., Shuvalov, V.A.

“…Sub-picosecond oscillations in the B L band were found in native and B M-modified reaction centers of Rhodobacter sphaeroides R26 at 293 K using 30 fs…”
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Evidence that Ala M260 is hydrogen-bonded to the reduced primary acceptor quinone QA−. in reaction centers of Rb. sphaeroides by Spoyalov, A.P., Hulsebosch, R.J., Shochat, S., Gast, P., Hoff, A.J.

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Jan Amesz: 11.03.1934–29.01.2001 by Hoff, A.J, Aartsma, T.J

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Asymmetric binding of the 1‐ and 4‐C=O groups of QA in Rhodobacter sphaeroides R26 reaction centres monitored by Fourier transform infra‐red spectroscopy using site‐specific isotopically labelled ubiquinone‐10 by Brudler, R., Groot, H.J., Liemt, W.B., Steggerda, W.F., Esmeijer, R., Gast, P., Hoff, A.J., Lugtenburg, J., Gerwert, K.

“…Using 1‐, 2‐, 3‐ and 4‐13C site‐specifically labelled ubiquinone‐10, reconstituted at the QA site of Rhodobacter sphaeroides R26 reaction centres, the…”
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Probing the energy landscape of bacterial photosynthetic reaction centers at cryogenic temperatures by ESEEM of spin-polarised D+QA− radical pairs by Dzuba, S.A., Gast, P., Hoff, A.J.

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Evidence that Ala M260 is hydrogen-bonded to the reduced primary acceptor quinone Q A−. in reaction centers of Rb. sphaeroides by Spoyalov, A.P., Hulsebosch, R.J., Shochat, S., Gast, P., Hoff, A.J.

“…The binding of the primary quinone anion radical Q A −. in reaction centers (Rcs) of Rhodobacter (Rb.) sphaeroides species was investigated with electron spin…”
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Spin-correlated radical pairs: microwave pulse effects on lifetimes, electron spin echo envelope modulations, and optimum conditions for detection by electron spin echo spectroscopy by Timmel, C.R., Fursman, C.E., Hoff, A.J., Hore, P.J.

“…A theoretical description is presented of the use of electron spin echo spectroscopy to study the spin-correlated radical pairs encountered in photosynthetic…”
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Influence of KF, DCMU and removal of Ca + on the high-spin EPR signal of the cytochrome b-559 heme Fe(III) ligated by OH − in chloroplasts by Hulsebosch, R.J., Hoff, A.J., Shuvalov, V.A.

“…An EPR signal at g = 6.8 attributed to the cytochrome (Cyt) b-559 heme Fe(III) ligated by OH − (Fiege, R., Schrieber, U., Lubitz, W., Renger, G. and Shuvalov,…”
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FTIR spectroscopy shows weak symmetric hydrogen bonding of the QB carbonyl groups in Rhodobacter sphaeroides R26 reaction centres by Brudler, R., de Groot, H.J.M., van Liemt, W.B.S., Gast, P., Hoff, A.J., Lugtenburg, J., Gerwert, K.

“…The absorption frequencies of the C = O and C = C (neutral state) and of the C̲⋯O (semiquinone state) stretching vibrations of QB have been assigned by FTIR…”
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Light-induced structural changes in photosynthetic reaction centres studied by ESEEM of spin-correlated D+QA− radical pairs by Borovykh, I.V., Dzuba, S.A., Proskuryakov, I.I., Gast, P., Hoff, A.J.

“…Zn-substituted Rhodobacter sphaeroides R26 reaction centres (RCs) frozen in the dark and under illumination exhibit quite different recombination kinetics of…”
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