Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Maarten P. Heyn"'
Autor:
J. Fitch, Terry E. Meyer, Berthold Borucki, Michael A. Cusanovich, Maarten P. Heyn, Sven Seibeck, John Kyndt
Publikováno v:
Biochemistry. 49:1744-1754
Ppr is a unique bacteriophytochrome that bleaches rather than forming a far-red-shifted Pfr state upon red light activation. Ppr is also unusual in that it has a blue light photoreceptor domain, PYP, which is N-terminally fused to the bacteriophytoch
Autor:
Terry E. Meyer, Chandra P. Joshi, Michael A. Cusanovich, Daniel Hoersch, Maarten P. Heyn, Harald Otto
Publikováno v:
Biochemistry. 48:9980-9993
In the Y42F mutant of photoactive yellow protein (PYP) the photoreceptor is in an equilibrium between two dark states, the yellow and intermediate spectral forms, absorbing at 457 and 390 nm, respectively. The nature of this equilibrium and the light
Publikováno v:
Biochemistry. 47:11518-11527
The transient changes of the tryptophan fluorescence of bovine rhodopsin in ROS membranes were followed in time from 1 micros to 10 s after flash excitation of the photoreceptor. Up to about 100 micros the fluorescence did not change, suggesting that
Publikováno v:
European Journal of Biochemistry. 147:483-487
Photoaffinity labeling of membrane-bound nicotinic acetylcholine receptor from Torpedo marmorata electric tissue with the ion-channel blocker [3H]TPMP+ reveals various functional states of the receptor protein if labeling is performed with ms time re
Autor:
Stephan Moltke, Michael F. Brown, Suhkmann Kim, Gilmar F. Salgado, Ingrid Wallat, Constantin Job, Maarten P. Heyn, Alexander A. Nevzorov, Andrey V. Struts, Koji Nakanishi
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1768:2979-3000
Solid-state 2H NMR spectroscopy gives a powerful avenue to investigating the structures of ligands and cofactors bound to integral membrane proteins. For bacteriorhodopsin (bR) and rhodopsin, retinal was site-specifically labeled by deuteration of th
Publikováno v:
Biophysical Journal. 91:2991-3001
The signaling state of the photoreceptor photoactive yellow protein is the long-lived intermediate I(2)'. The pH dependence of the equilibrium between the transient photocycle intermediates I(2) and I(2)' was investigated. The formation of I(2)' from
Autor:
Maarten P. Heyn, Chandra P. Joshi, Berthold Borucki, Michael A. Cusanovich, Harald Otto, Terry E. Meyer
Publikováno v:
Biochemistry. 45:7057-7068
Since the habitat of Halorhodospira halophila is distinctly alkaline, we investigated the kinetics and intermediates of the photocycle and photoreversal of the photoreceptor photoactive yellow protein (PYP) from pH 8 to 11. SVD analysis of the transi
Autor:
Michael A. Cusanovich, Maarten P. Heyn, Harald Otto, Berthold Borucki, Terry E. Meyer, Chandra P. Joshi
Publikováno v:
Biochemistry. 44:656-665
We investigated the kinetics of photoreversal from the I(1) and I(2) intermediates of photoactive yellow protein (PYP) by time-resolved optical absorption spectroscopy with double flash excitation. A first flash, at 430 nm, initiated the photocycle.
Publikováno v:
The Journal of Physical Chemistry B. 109:629-633
The absorption and CD spectra of wild-type PYP, apo-PYP, and the mutants, E46Q and M100A, were measured between 250 and 550 nm. At neutral pH, the two very weak absorption bands of wild-type PYP at 307 and 318 nm (epsilon(max) = 600 +/- 100 M(-1) cm(
Publikováno v:
The Journal of Physical Chemistry B. 108:2076-2086
Transient linear dichroism and linear birefringence changes in the photocycle of bacteriorhodopsin at alkaline pH were measured with magnetically oriented purple membrane samples using the method o...