Journal
BIOCHEMISTRY
Volume 54, Issue 18, Pages 2802-2805Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.5b00307
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Funding
- Sokol Institute of Pharmaceutical Life Sciences
- Montclair State University
- Montclair State University Sokol Faculty Student Research Program
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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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