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Photochemical and thermal stability of green and blue proteorhodopsins: implications for protein-based bioelectronic devices.

The journal of physical chemistry. B (2010-10-23)
Matthew J Ranaghan, Sumie Shima, Lavosier Ramos, Daniel S Poulin, Gregg Whited, Sanguthevar Rajasekaran, Jeffery A Stuart, Arlene D Albert, Robert R Birge
ABSTRACT

The photochemical and thermal stability of the detergent-solubilized blue- and green-absorbing proteorhodpsins, BPR and GPR, respectively, are investigated to determine the viability of these proteins for photonic device applications. Photochemical stability is studied by using pulsed laser excitation and differential UV-vis spectroscopy to assign the photocyclicity. GPR, with a cyclicity of 7 × 10(4) photocycles protein(-1), is 4-5 times more stable than BPR (9 × 10(3) photocycles protein(-1)), but is less stable than native bacteriorhodopsin (9 × 10(5) photocycles protein(-1)) or the 4-keto-bacteriorhodopsin analogue (1 × 10(5) photocycles protein(-1)). The thermal stabilities are assigned by using differential scanning calorimetry and thermal bleaching experiments. Both proteorhodopsins display excellent thermal stability, with melting temperatures above 85 °C, and remain photochemically stable up to 75 °C. The biological relevance of our results is also discussed. The lower cyclicity of BPR is found to be adequate for the long-term biological function of the host organism at ocean depths of 50 m or more.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Octyl β-D-glucopyranoside, ≥98% (GC)
Sigma-Aldrich
Octyl β-D-glucopyranoside, BioXtra, ≥98% (GC)
Sigma-Aldrich
Octyl β-D-glucopyranoside solution, ≥95% (HPLC), 50 % (w/v) in H2O
Sigma-Aldrich
Octyl-β-D-glucopyranoside 100 mM solution
Sigma-Aldrich
Octyl α-D-glucopyranoside, ≥98% (GC)