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Elucidation of the substrate recognition mechanism of VcCry1 (550.2)
Author(s) -
Ahmad Rohe,
Gindt Yvonne
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.550.2
Subject(s) - isothermal titration calorimetry , photolyase , dna , substrate (aquarium) , biophysics , chemistry , dna repair , biochemistry , biology , ecology
Isothermal titration calorimetry will be used to study the temperature dependence of DNA binding to Vibrio cholerae cryptochrome 1 (VcCry1), a DNA repair enzyme. VcCry1 uses light‐driven electron transfer to repair UV damaged single strand DNA but not double strand DNA. The enzyme is a good model to study substrate binding, since the repair process requires absorption of light and is separated from the damage recognition process. VcCry1 has an active site FAD which is required for substrate binding and repair. The thermodynamics along with the quantification of the electrostatic and nonelectrostatic interactions important in the VcCry1 substrate binding will be examined and compared to DNA photolyase, a related DNA repair enzyme that binds double stranded DNA. Grant Funding Source : Supported by The Margaret and Herman Sokol Institute for Pharmaceutical Life Sciences