Molecular Beam and ab Initio Studies of Photoactive Yellow Protein Chromophores: Influence of the Thioester Functionality and Single Bond Rotation-Reference-Cited by-同舟云学术

Molecular Beam and ab Initio Studies of Photoactive Yellow Protein Chromophores: Influence of the Thioester Functionality and Single Bond Rotation

Published:2014-10-17 Issue:43 Volume:118 Page:12395-12403
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Tan Eric M. M.¹,Amirjalayer Saeed¹²,Mazzella Paul¹,Bakker Bert H.¹,van Maarseveen Jan H.¹,Bieraugel Hans¹,Buma Wybren J.¹

Affiliation:

1. van ’t Hoff Institute for Molecular Sciences, Faculty of Science, University of Amsterdam, Science Park 904, 1098XH Amsterdam, The Netherlands

2. Physical Institute and Center for Nanotechnology (CeNTech) Westfälische Wilhelms-Universität Münster, Wilhelm-Klemm-Str. 10, 48149 Münster, Germany

Funder

Nederlandse Organisatie voor Wetenschappelijk Onderzoek

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp5075169

Reference40 articles.

1. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila

2. Single-molecule detection of structural changes during Per-Arnt-Sim (PAS) domain activation

3. Crystallographic structure of a photoreceptor protein at 2.4 A resolution

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

5. Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin

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