Abstract
EVER since Mirsky1 suggested that the bleaching of rhodopsin by light involves the reversible denaturation of its protein moiety, opsin, analogies have been drawn between bleaching and denaturation of the visual pigments. This notion derives its strongest experimental support from the apparent agreement between the minimum size of quantum required to bleach frog or cattle rhodopsin with light2 (48,500 cal./mole) and the Arrhenius activation energy (E a) for the thermal bleaching of frog rhodopsin3 (44,000 cal./mole). We find that this analogy breaks down on closer examination, and that light and heat bleach rhodopsin by different mechanisms, yielding different products.
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HUBBARD, R. Bleaching of Rhodopsin by Light and by Heat. Nature 181, 1126 (1958). https://doi.org/10.1038/1811126a0
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DOI: https://doi.org/10.1038/1811126a0
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