کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5373819 | 1504239 | 2013 | 10 صفحه PDF | دانلود رایگان |
- Lyophilizing of NgPAC2 from Naegleria gruberi caused loss of BLUF domain activity.
- Photo-induced tyrosine to flavin electron transfer in lyophilized NgPAC2.
- Photo-induced Tyr-Tyr cross-linking to o,oâ²-dityrosine in lyophilized NgPAC2.
- Photo-induced partial flavin cofactor reduction in lyophilized NgPAC2.
- Two NgPAC2 conformations with fast and slow photo-induced electron transfer.
The absorption and emission spectroscopic behavior of lyophilized photo-activated adenylate cyclase NgPAC2 from the amoeboflagellate Naegleria gruberi NEG-M strain consisting of a BLUF domain (BLUF = Blue Light sensor Using Flavin) and a cyclase homology domain was studied in the dark, during blue-light exposure and after blue-light exposure at a temperature of 4 °C. The BLUF domain photo-cycle dynamics observed for snap-frozen NgPAC2 was lost by lyophilization (no signaling state formation with flavin absorption red-shift). Instead, blue-light photo-excitation of lyophilized NgPAC2 caused sterically restricted Tyr-Tyr cross-linking (o,oâ²-ditysosine formation) and partial flavin cofactor reduction.
Journal: Chemical Physics - Volume 423, 23 September 2013, Pages 192-201