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Sci. Signal., 11 September 2012
Vol. 5, Issue 241, p. ec242
[DOI: 10.1126/scisignal.2003589]

EDITORS' CHOICE

Biochemistry Responding to Light and Heat

Valda Vinson

Science, AAAS, Washington, DC 20005, USA

The protein rhodopsin is sensitive to dim light, but its sensitivity is limited by signals caused by the noise of thermal activation. The basis of this relationship, known as the Barlow correlation, has long been debated. A recent study suggested that thermal activation involves a canonical isomerization reaction. Gozem et al. confirm that isomerization is the rate-limiting step controlling thermal noise, and they provide a molecular understanding of the Barlow correlation. They use quantum mechanics coupled with molecular mechanics to show that the transition state mediating thermal activation has the same electronic structure as the photochemical excited state.

S. Gozem, I. Schapiro, N. Ferré, M. Olivucci, The molecular mechanism of thermal noise in rod photoreceptors. Science 337, 1225–1228 (2012). [Abstract] [Full Text]

Citation: V. Vinson, Responding to Light and Heat. Sci. Signal. 5, ec242 (2012).

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