Deborah A. Berthold

senior staff scientist

Deborah Berthold (Ph.D., Duke University, 1990) is a senior research scientist whose main interests concern the structure and function of membrane proteins, especially those that contain a quinone binding site. Her long-term research project involves the alternative oxidase, a respiratory enzyme containing a carboxylate-bridged diiron center at its active site. The alternative oxidase is found in plants as well as the human pathogens, Trypanosoma sp. and Cryptosporidium parvum. Currently Deborah's research is focused determining the structure of the transmembrane protein DsbB by SSNMR. This quinone reductase is one component of a pathway that is responsible for forming disulfide bonds in proteins of the E. coli periplasm. Deborah has developed new and improved methods for efficient expression and purification of isotopically labeled membrane proteins while learning NMR data acquisition and analysis techniques.

laboratory protocols

Top Ten Tips for Producing ¹³C,¹⁵N Protein in Abundance (CIL Application Note #15)

Other CIL Application Notes

key publications (pubmed)

“Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy”, Li, Y.; Berthold, D. A.; Gennis, R. B.; Rienstra, C. M. Protein Sci. (Accelerated Publication) 2008, 17, 199-204. (Published online, February 1, 2008).

“High-yield expression and purification of isotopically labeled cytochrome P450 monooxygenases for solid-state NMR spectroscopy”, Rupasinghe, S. G.; Duan, H.; Frericks Schmidt, H. L.; Berthold, D. A.; Rienstra, C. M.; Schuler, M. A, Biochim. Biophys. Acta Biomembr. 2007, 1768, 3061-3070. (Published online, September 25, 2007).

“Partial ¹³C and ¹⁵N chemical shift assignments of the disulfide bond forming enzyme DsbB by 3D magic-angle spinning NMR spectroscopy”, Li, Y.; Berthold, D. A.; Frericks, H. L.; Gennis, R. B.; Rienstra, C. M., ChemBioChem 2007, 8, 434-442. (Published online February 7, 2007).

“Membrane-bound dirron carboxylate proteins”, Berthold, D. A.; Stenmark, P., Annu. Rev. Plant Biol. 2003, 54, 497-517. (Published online June 2003).

"EPR studies of the mitochrondrial alternative oxidase: Evidence for a diiron carboxylate center", Berthold, D. A.; Voevodskaya, M.; Stenmark, P.; Graeslund, A.; Nordlund, P., J. Biol. Chem. 2002, 277, 43608-43614. (Published online September 4, 2002).

“A new member of the family of di-iron carboxylate proteins: Coq7 (clk-1), a membrane-bound hydroxylase involved in ubiquinone biosynthesis”, Stenmark, P.; Gruenler, J.; Mattsson, J.; Sindelar, P. J.; Nordlund, P.; Berthold, D. A., J. Biol. Chem. 2001, 276, 33297-33300. (Published online July 2, 2001).

“New insight into the structure and function of the alternative oxidase”, Berthold, D. A.; Andersson, M. E.; Nordlund, P., Biochim. Biophys. Acta 2000 1460, 241-254. (Available online November 20, 2000).

“Isolation of mutants of the Arabidopsis thaliana alternative oxidase (ubiquinol:oxygen oxidoreductase) resistant to salicylhydroxamic acid”, Berthold, D. A., Biochim. Biophys. Acta 1998, 1364, 73-83. (Available online October 16, 1998).

“Partial purification of the cyanide-resistant alternative oxidase of skunk cabbage (Symplocarpus foetidus) mitochondria”, Berthold, D. A.; Siedow, J. N., Plant Physiol. 1993, 101, 113-119. (Available online).

“Determination of molecular mass of the aroid alternative oxidase by radiation inactivation analysis”, Berthold, D. A.; Fluke, D. J.; Siedow, J. N., Biochem. J. 1988, 252, 73-77. (Available online).

“A highly resolved, oxygen-evolving photosystem II preparation from spinach thylakoid membranes: EPR and electron-transport properties”, Berthold, D. A.; Babcock, G. T.; Yocum, C. F., Febs Lett. 1981, 134, 231-234. (Available online).