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Use of Engineered Unique Cysteine Residues to Facilitate Oriented Coupling of Proteins Directly to a Gold Substrate
Author(s) -
Magis Gerhard J.,
Olsen John D.,
Reynolds Nicholas P.,
Leggett Graham J.,
Hunter C. Neil,
Aartsma Thijs J.,
Frese Raoul N.
Publication year - 2011
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.2011.00948.x
Subject(s) - periplasmic space , rhodobacter sphaeroides , cysteine , chemistry , substrate (aquarium) , transmembrane protein , biophysics , monolayer , coupling (piping) , colloidal gold , covalent bond , nanotechnology , biochemistry , materials science , nanoparticle , enzyme , organic chemistry , biology , receptor , ecology , photosynthesis , escherichia coli , metallurgy , gene
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.