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Resonanz-Raman-Spektroskopie als Methode zur Untersuchung des aktiven Zentrums von Hydrogenasen.
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- Angewandte Chemie, 2013, v. 125, n. 19, p. 5267, doi. 10.1002/ange.201209732
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Rücktitelbild: Resonanz-Raman-Spektroskopie als Methode zur Untersuchung des aktiven Zentrums von Hydrogenasen (Angew. Chem. 19/2013).
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- Angewandte Chemie, 2013, v. 125, n. 19, p. 5294, doi. 10.1002/ange.201302121
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- Article
Common Structural Elements in the Chromophore Binding Pocket of the Pfr State of Bathy Phytochromes.
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- Photochemistry & Photobiology, 2017, v. 93, n. 3, p. 724, doi. 10.1111/php.12742
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Fourier transform near-infrared resonance Raman spectroscopic study of the α-subunit of phycoerythrocyanin and phycocyanin from the cyanobacterium Mastigocladus laminosus.
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- Journal of Raman Spectroscopy, 1998, v. 29, n. 10/11, p. 939, doi. 10.1002/(SICI)1097-4555(199810/11)29:10/11<939::AID-JRS320>3.0.CO;2-X
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Time-resolved rapid-scan Fourier transform infrared difference spectroscopy on a noncyclic photosystem: Rhodopsin photointermediates from Lumi to Meta II.
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- Biopolymers, 2006, v. 83, n. 2, p. 159, doi. 10.1002/bip.20540
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Preface.
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- Biopolymers, 2006, v. 82, n. 4, p. 285, doi. 10.1002/bip.20528
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Fourier transform IR spectroscopy study for new insights into molecular properties and activation mechanisms of visual pigment rhodopsin.
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- Biopolymers, 2003, v. 72, n. 3, p. 133, doi. 10.1002/bip.10407
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- Article
A protonation-coupled feedback mechanism controls the signalling process in bathy phytochromes.
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- Nature Chemistry, 2015, v. 7, n. 5, p. 423, doi. 10.1038/nchem.2225
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- Article
Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases.
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- Angewandte Chemie International Edition, 2013, v. 52, n. 19, p. 5162, doi. 10.1002/anie.201209732
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- Article
Back Cover: Resonance Raman Spectroscopy as a Tool to Monitor the Active Site of Hydrogenases (Angew. Chem. Int. Ed. 19/2013).
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- Angewandte Chemie International Edition, 2013, v. 52, n. 19, p. 5186, doi. 10.1002/anie.201302121
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- Article
The Photoreactions of Recombinant Phytochrome CphA from the Cyanobacterium Calothrix PCC7601: A Low-Temperature UV–Vis and FTIR Study.
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- Photochemistry & Photobiology, 2009, v. 85, n. 1, p. 239, doi. 10.1111/j.1751-1097.2008.00426.x
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- Article
Coupling of Protonation Switches During Rhodopsin Activation.
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- Photochemistry & Photobiology, 2007, v. 83, n. 2, p. 286, doi. 10.1562/2006-06-19-IR-937
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- Article
The Photoreactions of Recombinant Phytochrome from the Cyanobacterium Synechocystis: A Low-Temperature UV-Vis and FT-IR Spectroscopic Study.
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- Photochemistry & Photobiology, 2000, v. 71, n. 5, p. 655, doi. 10.1562/0031-8655(2000)0710655TPORPF2.0.CO2
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- Article
IDENTIFICATION OF THE PROTON ACCEPTOR OF SCHIFF BASE DEPROTONATION IN BACTERIORHODOPSIN: A FOURIER-TRANSFORM-INFRARED STUDY OF THE MUTANT ASP85 → GLU IN ITS NATURAL LIPID ENVIRONMENT.
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- Photochemistry & Photobiology, 1992, v. 56, n. 6, p. 1073, doi. 10.1111/j.1751-1097.1992.tb09731.x
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CONFORMATIONAL CHANGES OF CYTOSOLIC LOOPS OF BOVINE RHODOPSIN DURING THE TRANSITION TO METARHODOPSIN-II: AN INVESTIGATION BY FOURIER TRANSFORM INFRARED DIFFERENCE SPECTROSCOPY.
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- Photochemistry & Photobiology, 1992, v. 56, n. 1, p. 57, doi. 10.1111/j.1751-1097.1992.tb09602.x
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- Article
THE PHOTOREACTION OF THE DEIONIZED FORM OF THE PURPLE MEMBRANE INVESTIGATED BY FTIR DIFFERENCE SPECTROSCOPY.
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- Photochemistry & Photobiology, 1990, v. 51, n. 4, p. 459, doi. 10.1111/j.1751-1097.1990.tb01737.x
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- Article