Molecular eyes: proteins that transform light into biological information by John T. M. Kennis, and Tilo Mathes Interface Focus Volume 3(5): October 6, 2013 ©2013 by The Royal Society
Most biological photoreceptors can be described as light-activated switches, which thermally recover to the dark-adapted state. John T. M. Kennis, and Tilo Mathes Interface Focus 2013;3: ©2013 by The Royal Society
(a) BLUF domain of Slr1694 in dark- and light-adapted states illustrating the putative glutamine rotation mechanism. John T. M. Kennis, and Tilo Mathes Interface Focus 2013;3: ©2013 by The Royal Society
Photocycle of BLUF domains as observed by ultrafast vis/IR and fluorescence spectroscopy on Slr1694. John T. M. Kennis, and Tilo Mathes Interface Focus 2013;3: ©2013 by The Royal Society
(a) The hydrogen bond network between tyrosine, glutamine and the flavin determines light- induced proton-coupled electron transfer. John T. M. Kennis, and Tilo Mathes Interface Focus 2013;3: ©2013 by The Royal Society
Chemically modified BLUF domains. John T. M. Kennis, and Tilo Mathes Interface Focus 2013;3: ©2013 by The Royal Society
(a) Photocycle of BLUF domains as observed by ultrafast spectroscopy on redox-modulated Slr1694 proteins. John T. M. Kennis, and Tilo Mathes Interface Focus 2013;3: ©2013 by The Royal Society