Abstract
Flavodoxins are a family of FMN binding proteins widely distributed in prokaryotes. They involve in various electron transfer reactions using the non-covalently bound FMN cofactor as the redox center. The Escherichia coli yqcA gene was identified to encode a short-chain favodoxin based on sequence information. However, the structure of YqcA protein is unknown and its exact biological function in cell is yet to be investigated. Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of E. coli YqcA in both the apo and holo states.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
