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• W3133846989 startingPage "1473" @default.
• W3133846989 abstract "The blue light‐regulated phosphodiesterase BlrP1 from Klebsiella pneumoniae hydrolyzes cyclic dimeric guanosine monophosphate (GMP) in a blue light‐dependent manner. It contains a photosensing BLUF domain and a functional EAL domain. Previously, it was reported that conformational changes in the dimer upon light illumination occurred only when both protomers of the dimer were excited. Based on this observation, it was proposed that BlrP1 might be a nonlinear light intensity sensor. To test this, here, the correlation between the turnover number of the hydrolysis reaction ( k cat ) and the fraction of the excited protein ( f red ) was measured by simultaneously monitoring the reaction rate and f red . Our results show that k cat is proportional to f red 2 . Thus, BlrP1 works as a nonlinear light intensity sensor to sense a strong light environment." @default.
• W3133846989 created "2021-03-15" @default.
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• W3133846989 date "2021-03-23" @default.
• W3133846989 modified "2023-10-02" @default.
• W3133846989 title "Enzymatic activity of the blue light‐regulated phosphodiesterase BlrP1 from <i>Klebsiella pneumoniae</i> shows a nonlinear dependence on light intensity" @default.
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• W3133846989 doi "https://doi.org/10.1002/1873-3468.14073" @default.
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