Published Paper

Meriçs’ paper titled “Identification and characterization of a new class of (6-4) photolyase from Vibrio cholerae” is published in Biochemistry. 58(43):4352-4360. doi: 10.1021/acs.biochem.9b00766.

Figure 1
Purification and spectroscopic analysis of recombinant V. cholerae iron–sulfur bacterial cryptochromes and photolyases (FeS-BCP). (A) Coomassie staining. Purified VCA0809 and the cell free extract (CFE) of E. coli expressing MBP-Vc(6–4)FeS-BCP were separated via 10% SDS–PAGE and visualized by being stained with Coomassie Brilliant Blue: L, ladder; Un, uninduced CFE; In, induced CFE; (6–4), MBP-Vc(6–4) FeS-BCP fusion protein. (B) Absorption spectra of Vc(6–4) MBP-FeS-BCP protein from 250 to 750 nm. The inset shows the expanded scale of the absorption spectrum from 300 to 700 nm. Fluorescence spectra of MBP-Vc(6–4) FeS-BCP with (C) folate and (D) flavin excitation emission wavelengths.