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Updated: Apr 14, 2026

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
Published on: March 31, 2010
Binding of Substrate Locks the Electrochemistry of CRY-DASH into DNA Repair
Yvonne M Gindt1, Adriana Messyasz1, Pamela I Jumbo1
1Department of Chemistry and Biochemistry, Montclair State University, Montclair, New Jersey 07043, United States.
Abstract:
VcCry1, a member of the CRY-DASH family, may serve two diverse roles in vivo, including blue-light signaling and repair of UV-damaged DNA. We have discovered that the electrochemistry of the flavin adenine dinucleotide cofactor of VcCry1 is locked to cycle only between the hydroquinone and neutral semiquinone states when UV-damaged DNA is present. Other potential substrates, including undamaged DNA and ATP, have no discernible effect on the electrochemistry, and the kinetics of the reduction is unaffected by damaged DNA. Binding of the damaged DNA substrate determines the role of the protein and prevents the presumed photochemistry required for blue-light signaling.
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