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Wouter D. Hoff

Researcher at Oklahoma State University–Stillwater

Publications -  95
Citations -  4503

Wouter D. Hoff is an academic researcher from Oklahoma State University–Stillwater. The author has contributed to research in topics: Chromophore & Genome. The author has an hindex of 35, co-authored 92 publications receiving 4273 citations. Previous affiliations of Wouter D. Hoff include Florida State University College of Arts and Sciences & Albert Einstein College of Medicine.

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Journal ArticleDOI

The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein.

TL;DR: To the authors' knowledge, this is the first report of a true repellent response to light in a free-swimming eubacterium, since the blue light response in Escherichia coli and Salmonella typhimurium is unlikely to be a sensory process.
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Molecular mechanism of photosignaling by archaeal sensory rhodopsins

TL;DR: The SR-Htr signaling complexes allow studies of the biophysical chemistry of signal generation and relay, from the photobiophysics of initial excitation of the receptors to the final output at the level of the flagellar motor switch, revealing fundamental principles of sensory transduction.
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Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry

TL;DR: PYP is the first example of a protein containing p-coumaric acid, a metabolite previously found only in plants, as a prosthetic group and establishes the photoactive yellow proteins as a new type of photochemically active receptor molecule.
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Measurement and global analysis of the absorbance changes in the photocycle of the photoactive yellow protein from Ectothiorhodospira halophila

TL;DR: Global analysis of the data established that in the time domain between 5 ns and 2 s only two intermediates are involved in the room temperature photocycle of PYP, as has been proposed before.
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Evidence for trans-cis isomerization of the p-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein

TL;DR: The data presented here establish the photo‐isomerization of the vinyl double bond in the chromophore yellow protein, a eubacterial photosensory protein, offering an explanation for the strong spectroscopic similarities between photoactive yellow protein and the sensory rhodopsins.