Journal
PHOTOCHEMISTRY AND PHOTOBIOLOGY
Volume 87, Issue 5, Pages 1050-1057Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1751-1097.2011.00948.x
Keywords
-
Categories
Funding
- Biotechnology and Biological Sciences Research Council (UK)
- Photosynthetic Antenna Research Center (PARC)
- Energy Frontier Research Center
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-SC 0001035]
- EPSRC
- Dutch Science Organization NWO
- Biotechnology and Biological Sciences Research Council [BB/G021546/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/C523857/1] Funding Source: researchfish
- BBSRC [BB/G021546/1] Funding Source: UKRI
Ask authors/readers for more resources
A prerequisite for any lab on a chip device that utilizes an electrical signal from the sensor protein is the ability to attach the protein in a specific orientation onto a conducting substrate. Here, we demonstrate the covalent attachment to a gold surface of light-harvesting membrane proteins, from Rhodobacter sphaeroides, via cysteine (Cys) residues engineered on either the cytoplasmic or periplasmic face. This simple directed attachment is superior in its ability to retain light-harvesting complex (LHC) function, when compared to a similar attachment procedure utilizing a self-assembled monolayer on gold. LH 1 has previously been observed to have superior photostability over LH 2 (Magis et al. [2010] Biochim. Biophys. Acta, 1798, 637-645); this characteristic is maintained even with the introduction of Cys residues.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available