Photo-dynamics of the lyophilized photo-activated adenylate cyclase NgPAC2 from the amoeboflagellate Naegleria gruberi NEG-M strain

Penzkofer, A. and Tanwar, M. and Veetil, S. K. and Kateriya, S. and Stierl, M. and Hegemann, P. (2013) Photo-dynamics of the lyophilized photo-activated adenylate cyclase NgPAC2 from the amoeboflagellate Naegleria gruberi NEG-M strain. CHEMICAL PHYSICS, 423. pp. 192-201. ISSN 0301-0104,

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Abstract

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 degrees 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, o'-ditysosine formation) and partial flavin cofactor reduction. (C) 2013 Elsevier B. V. All rights reserved.

Item Type: Article
Uncontrolled Keywords: BLUE-LIGHT PHOTORECEPTOR; ELECTRON-TRANSFER; RHODOBACTER-SPHAEROIDES; INFRARED-SPECTROSCOPY; AQUEOUS-SOLUTION; AMINO-ACIDS; PROTEIN; FLAVIN; DOMAIN; TYROSINE; Lyophilized photo-activated cyclase NgPAC2; BLUF domain; Amoeboflagellate Naegleria gruberi; Flavin; Tyr-Tyr cross-linking; o,o '-Dityrosine; Fluorescence quenching; Flavin reduction
Subjects: 500 Science > 530 Physics
Divisions: Physics > Institute of Experimental and Applied Physics > Alumni or Retired Professors > Group Alfons Penzkofer
Depositing User: Dr. Gernot Deinzer
Date Deposited: 31 Mar 2020 12:01
Last Modified: 31 Mar 2020 12:01
URI: https://pred.uni-regensburg.de/id/eprint/16020

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