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Trends in Applied Spectroscopy   Volumes    Volume 11 
Photo-dynamics of photoactivated adenylyl cyclase LiPAC from the spirochete bacterium Leptonema illini strain 3055T
Alfons Penzkofer, Meenakshi Tanwar, Sindhu Kandoth Veetil, Suneel Kateriya
Pages: 39 - 62
Number of pages: 24
Trends in Applied Spectroscopy
Volume 11 

Copyright © 2014 Research Trends. All rights reserved

The photoactivated adenylyl cyclase from the spirochete bacterium Leptonema illini, abbreviated LiPAC, was synthesized and characterized by absorption and fluorescence spectroscopic methods. LiPAC consists of a BLUF (Blue Light sensor Using Flavin) domain and an adenylyl cyclase homology domain (CHD). Photo-excitation of fully oxidized flavin Flox in LiPAC resulted in a typical primary (dark-adapted) BLUF domain photo-cycle dynamics. The quantum efficiency of BLUF domain signaling state formation was determined to be Φs ≈ 0.60. Continued blue-light-excitation of LiPAC in the light-adapted state caused irreversible photo-degradation of non-covalently bound Flox to covalently bound fully reduced flavin Flred with a quantum efficiency of ΦD ≈ 1.1 × 10-5. At 20 °C the time constant of signaling state recovery to the receptor state after excitation light switch-off was τrec ≈ 2.6 s. The protein thermal stability was studied by stepwise sample heating and cooling. An apparent LiPAC melting temperature of 54 °C was determined. Schemes of the primary BLUF domain photo-cycling dynamics and the secondary BLUF domain photo-degradation in the signaling state are presented.
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