Professor of Biology
Ph.D., Dr. Eng.,1977, University Louis Pasteur (Microbiology)


Office:
103B Lynch Laboratory
Tel: 215-898-4394

Lab:
111 Lynch Laboratory
Tel: 215-898-8394

Fax: 215-898-8780
Email: fdaldal@sas.upenn.edu

Daldal homepage

Our work is focused on the structure, function, assembly, biogenesis and regulation in response to environmental signals (light and oxygen) of multi-subunit, prosthetic groups bearing membrane proteins involved in cellular energy transduction (photosynthesis and respiration) pathways. These proteins are vital for important cellular functions that extend from ATP synthesis to secretion, solute transport, motility and thermogenesis. Their dysfunction severely compromises cellular energy production, and leads to neurological and muscular diseases in humans, or to lower crop yields in plants. We employ molecular genetic and genomic/proteomic approaches in combination with molecular biological, biochemical, biophysical and structural techniques, and we work with the purple non-sulfur facultative photosynthetic bacterium Rhodobacter capsulatus as a model organism instead of eukaryotic organelles that are more refractory to multidisciplinary analyses. Ongoing research involves the cytochrome bc1 complex, the cytochrome cbb3 oxidase and their physiological electron carriers.

Selected Publications:

Onder, O., H. Yoon, B. Naumann, M. Hippler, A. Dancis and F. Daldal (2006) Modifications of the lipoamide-containing mitochondrial subproteome in a yeast mutant defective in cysteine desulfurase. Mol Cell Proteomics (in press.)

Aygun, S., S. Mandaci, H.-G. Koch, H. Goldfine and F. Daldal (2006) Ornithine lipids are required for membrane cytochrome complexes. Molec. Microbiol. 61:418-435.

Lee. D.-W., Y. Ozturk, A. Mamedova, A., Osyczka, J.W. Cooley and F. Daldal (2006) A functional hybrid between the cytochrome bc1 complex and its physiological membrane anchored electron acceptor cyt cy in R. capsulatus. Biochim. Biophys. Acta 1757:346-352.

Turkarslan, S., C. Sanders and F. Daldal (2006) Extracytoplasmic prosthetic group ligation to apoproteins: maturation of c-type cyts. Molec. Microbiol. 60:537-541.

Kulajta, C., J.O. Thumfart, S. Haid, F. Daldal and H.-G. Koch (2006) Multi-step assembly pathway of the cbb3-type cyt c oxidase complex. J. Mol. Biol. 355:989-1004.

Cooley, J.W., T. Ohnishi and F. Daldal (2005) Binding dynamics at the quinone reduction (Qi) site influence the equilibrium interactions of the iron sulfur protein and hydroquinone oxidation (Qo) site of the cyt bc1 complex. Biochemistry 44:10520-10532.

Mather, M.W., E. Darrouzet, M. Valkova-Valchanova, J.W. Cooley, M.T. McIntosh, F. Daldal and A. B. Vaidya (2005) Uncovering the molecular mode of action of the antimalarial drug atovaquone using a bacterial system. J. Biol.Chem. 280:27458-27465.

Sanders, C., M. Deshmukh, D. Astor, R.G. Kranz and F. Daldal (2005) Overproduction of CcmG and CcmFHRc fully suppresses the c-type cytochrome biogenesis defect of R. capsulatus CcmI-null mutants. J. Bacteriol 187:4245-4256.

Berry, E. A., L.-S. Huang, N.G.,Pon, Valkova- Valchanova, M., and F. Daldal (2004) X-ray structure of Rhodobacter capsulatus cytochrome bc1: Comparison with its mitochondrial and chloroplast counterparts. Photosyn. Res. 81:251-275.

Cooley, J. W., A.G. Roberts, M.K. Bowman, D.K. Kramer and F. Daldal (2004) Raised midpoint potential of the [2Fe2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S protein subunit. Biochemistry 43:2217-2227.