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Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction.
This work determined crystal structures of the dark-adapted state and of a photo-excited, red-shifted photocycle intermediate of the BLUF unit of AppA, a purple bacterial photoreceptor involved in the light-dependent regulation of photosynthesis gene expression. Expand
Crystal structure and mechanism of a DNA (6-4) photolyase.
Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction.
The structure of the dark resting state of BlrB, a short BLUF domain-containing protein from Rhodobacter sphaeroides, suggests a unique photochemical signaling switch in which the absorption of light induces a structural change in the rim surrounding the hook, thereby changing the protein interface between BLUF and the output domain. Expand
Molecular models predict light-induced glutamine tautomerization in BLUF photoreceptors.
Molecular models for the dark and light states of the BLUF domain of the Rhodobacter sphaeroides AppA protein are developed based on the crystal structures and quantum-mechanical simulations and light-induced isomerization of an amino acid residue instead of a chromophore represents a feature that has not been described previously in photoreceptors. Expand
Ultrafast infrared spectroscopy of riboflavin: dynamics, electronic structure, and vibrational mode analysis.
Femtosecond time-resolved infrared spectroscopy was used to study the vibrational response of riboflavin in DMSO to photoexcitation and reveals intra- and intermolecular hydrogen bonding of the rib oflavin chromophore. Expand
Structure and Mechanistic Implications of a Tryptophan Synthase Quinonoid Intermediate
The crystal structure of the indoline quinonoid intermediate of tryptophan synthase is presented and its implications for the enzymatic mechanism and allosteric regulation are discussed. Expand
Glutamine rotamers in BLUF photoreceptors: a mechanistic reappraisal.
Physical criteria for the dark and light state structures as well as for the light-activation process to evaluate existing models of BLUF using quantum-chemical calculations are proposed and it is demonstrated that the tautomerized glutamine is consistent with criteria and observations of the BLUF light state. Expand
Decrypting cryptochrome: revealing the molecular identity of the photoactivation reaction.
It is demonstrated that after photoexcitation aradical pair forms, becomes stabilized through proton transfer, and decays back to the protein's resting state on time scales allowing the protein, in principle, to act as a radical pair-based magnetic sensor. Expand
Photoreaction in BLUF Receptors: Proton‐coupled Electron Transfer in the Flavin‐Gln‐Tyr System †
The computed relaxation pathways reveal that the hydrogen bonds involving glutamine in the chromophore‐binding pocket control BLUF photoefficiency. Expand
Neutral histidine and photoinduced electron transfer in DNA photolyases.
  • T. Domratcheva
  • Chemistry, Medicine
  • Journal of the American Chemical Society
  • 16 November 2011
It is found that protonation of His365 in the presence of the hydroquinone-anion electron donor causes spontaneous, as opposed to photoinduced, coupled proton and electron transfer to the (6-4) photoproduct. Expand