1 research outputs found
Binding of Substrate Locks the Electrochemistry of CRY-DASH into DNA Repair
VcCry1, a member of the CRY-DASH
family, may serve two diverse
roles <i>in vivo</i>, 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