Next Article in Journal
Evaporation Rate of Water as a Function of a Magnetic Field and Field Gradient
Next Article in Special Issue
Why Flavins Are not Competitors of Chlorophyll in the Evolution of Biological Converters of Solar Energy
Previous Article in Journal / Special Issue
Bacterial Over-Expression and Purification of the 3'phosphoadenosine 5'phosphosulfate (PAPS) Reductase Domain of Human FAD Synthase: Functional Characterization and Homology Modeling
Article

Electrochemical Characterization of Escherichia coli Adaptive Response Protein AidB

1
Department of Chemistry, Boston University, 590 Commonwealth Ave., Boston, MA 02215, USA
2
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Ave., Cambridge, MA 02139, USA
3
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
4
Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
5
Center for Environmental Health, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
*
Author to whom correspondence should be addressed.
Present address: Johnson & Johnson Pharmaceutical Research & Development, 930 Route 202 South, Raritan, NJ 08869, USA
Int. J. Mol. Sci. 2012, 13(12), 16899-16915; https://doi.org/10.3390/ijms131216899
Received: 7 October 2012 / Revised: 26 November 2012 / Accepted: 3 December 2012 / Published: 11 December 2012
(This article belongs to the Special Issue Flavins)
When exposed to known DNA-damaging alkylating agents, Escherichia coli cells increase production of four DNA repair enzymes: Ada, AlkA, AlkB, and AidB. The role of three enzymes (Ada, AlkA, and AlkB) in repairing DNA lesions has been well characterized, while the function of AidB is poorly understood. AidB has a distinct cofactor that is potentially related to the elusive role of AidB in adaptive response: a redox active flavin adenine dinucleotide (FAD). In this study, we report the thermodynamic redox properties of the AidB flavin for the first time, both for free protein and in the presence of potential substrates. We find that the midpoint reduction potential of the AidB flavin is within a biologically relevant window for redox chemistry at −181 mV, that AidB significantly stabilizes the flavin semiquinone, and that small molecule binding perturbs the observed reduction potential. Our electrochemical results combined with structural analysis allow for fresh comparisons between AidB and the homologous acyl-coenzyme A dehydrogenase (ACAD) family of enzymes. AidB exhibits several discrepancies from ACADs that suggest a novel catalytic mechanism distinct from that of the ACAD family enzymes. View Full-Text
Keywords: adaptive response; DNA repair; protein electrochemistry; acyl-coenzyme A dehydrogenase; flavin cofactor; reduction potential adaptive response; DNA repair; protein electrochemistry; acyl-coenzyme A dehydrogenase; flavin cofactor; reduction potential
Show Figures

MDPI and ACS Style

Hamill, M.J.; Jost, M.; Wong, C.; Bene, N.C.; Drennan, C.L.; Elliott, S.J. Electrochemical Characterization of Escherichia coli Adaptive Response Protein AidB. Int. J. Mol. Sci. 2012, 13, 16899-16915. https://doi.org/10.3390/ijms131216899

AMA Style

Hamill MJ, Jost M, Wong C, Bene NC, Drennan CL, Elliott SJ. Electrochemical Characterization of Escherichia coli Adaptive Response Protein AidB. International Journal of Molecular Sciences. 2012; 13(12):16899-16915. https://doi.org/10.3390/ijms131216899

Chicago/Turabian Style

Hamill, Michael J., Marco Jost, Cintyu Wong, Nicholas C. Bene, Catherine L. Drennan, and Sean J. Elliott 2012. "Electrochemical Characterization of Escherichia coli Adaptive Response Protein AidB" International Journal of Molecular Sciences 13, no. 12: 16899-16915. https://doi.org/10.3390/ijms131216899

Find Other Styles

Article Access Map by Country/Region

1
Only visits after 24 November 2015 are recorded.
Back to TopTop