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15 August 2003 Bacteriorhodopsin as a chemical and biological sensor
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Bacteriorhodopsin (bR) is a small protein containing the chromophore retinal, and resides in the membrane of the Halobacterium salinarium. When the retinal absorbs a photon, a cycle of structural changes is triggered resulting in a cross-membrane proton transfer, which is used to generate energy for the organism. Many studies have been conducted to elucidate the dynamical structure - optical property relations, and the overall mechanism of photo-induced proton transport in bR is now well understood. On the other hand, site selective mutagenesis allows engineering of the original ("wild-type") bR, such that the protein can be made sensitive to specific chemicals or biological structures that consequently induce changes in the proton-transport. As such, bR provides a unique molecular platform onto which various functional elements can be built: peptide receptors for molecular recognition of pathogens (e.g. viruses, cancer cells, spores, bacteria, bio-toxins), fluorescent tags (using the inherent optical transduction mechanism of bR), and chemical anchors for capturing target cells. In particular, the stability of bR in extreme environments (pH range of 1 - 11, temperatures up to 110 °C) allows for optical detection under a large range of environmental conditions. In this paper we present and discuss experimental data of several bR mutants and their potential as chemical and biological sensors. In particular, the optical changes associated with metal ligand binding are discussed for two mutants, 170C and 169C/96N, as well as the optical changes associated with streptavidin-coated beads bound to bR with strep II tags inserted in the E/F loop.
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Bauke Heeg, Richard Needleman, Anatoliy Khizhnyak, Drew M. L'Esperance, Eddie Scott, Vladimir B. Markov, and James D. Trolinger "Bacteriorhodopsin as a chemical and biological sensor", Proc. SPIE 5085, Chemical and Biological Sensing IV, (15 August 2003);

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