David R. Benson
1251 Wescoe Hall Drive
Phone: (785) 864-4090
Fax: (785) 864-5396
- B.S., 1985, Pennsylvania State University
- Ph.D., 1990, University of California, Los Angeles
- National Institutes of Health Postdoctoral Fellow, 1990-1993, University of California, Berkeley.
Areas of Specialization
Hemoprotein Structure and Function
The chemistry and biochemistry of heme proteins.
Heme is an iron-containing macrocycle that is an integral component of many proteins in bacteria, plants and animals.It is the part of hemoglobin that gives blood its red color.Heme proteins participate in a wide array of biological processes, including transport and storage of dioxygen (hemoglobin and myoglobin, respectively), electron transport (b and c cytochromes), breakdown of hydrogen peroxide (peroxidases and catalases), and hydrocarbon oxidation (cytochrome P450).Several recently discovered heme proteins function as sensors for small molecules such as CO and O2.Part of our group’s research effort is directed toward design and synthesis of molecules that contain structural features common to these heme proteins, but which are smaller and therefore easier to study.We have adopted a multidisciplinary chemical approach to investigate how changes introduced into these model compounds influence their structure and function, in order that we may better understand how nature has fine-tuned the corresponding natural proteins to carry out their roles with remarkably high efficiency and specificity.Our studies of model heme proteins are complemented by investigations of their natural counterparts, projects which provide students with the opportunity to also learn some basic techniques of biochemistry and molecular biology.An example is cytochrome b5, an electron transfer protein found in animals and plants.
Cowley, A. B.; Benson, D. R. “Weak-field Anions Displace the Histidine Ligand in a Synthetic Heme Peptide, but not in N-Acetylmicroperoxidase-8: Possible Role of Heme Geometry Differences” Inorg. Chem. 2007, 46, 48-59.
Wang, L.; Cowley, A. B.; Terzyan, S.; Zhang, X.; Benson, D.R. “Comparison of Cytochromes b5 From Insects and Vertebrates.” Proteins: Struct. Funct. Bioinformat. 2007, 67, 293-304.
Cowley, A. B.; Kennedy, M. L.; Silchenko, S.; Lukat-Rodgers, G.; Rodgers, K.R.; Benson, D.R. “Insight into Heme Protein Redox Potential Control and Functional Aspects of Six-Coordinate Ligand-Sensing Heme Proteins from Studies of Synthetic Heme Peptides” Inorg. Chem. 2006, 45, 9985-10001.
Wang, L.; Sun, N.; Terzyan, S.; Zhang, X.; Benson, D.R. “A Histidine/Tryptophan π-Stacking Interaction Stabilizes the Heme-Independent Folding Core of Microsomal Apocytochrome b5 Relative to that of Mitochondrial Apocytochrome b5” Biochemistry 2006, 45, 13750-13759.
Cowley, A.B.; Sun, N.; Rivera, M.; Benson, D.R. “Divergence in Non-Specific Hydrophobic Packing Interactions in the Apo State, and its Possible Role in Functional Specialization of Mitochondrial and Microsomal Cytochrome b5” Biochemistry 2005, 44, 14606-14615.
Sun, N.; Wang, A.; Cowley, A.B.; Altuve, A.; Rivera, M.; Benson, D. R. “Enhancing Stability of Microsomal Cytochrome b5: A Rational Approach Informed by Comparative Studies with the Outer Mitochondrial Membrane Isoform” Protein Eng. Des. Select. 2005, 18, 571-579.
Cowley, A. B.; Rivera, M.; Benson, D. R. “Stabilizing Roles of Residual Structure in the Empty Heme Binding Pockets and Unfolded States of Microsomal and Mitochondrial Apocytochrome b5” Protein Sci.2004, 13, 2316-2329.
Cowley, A. B.; Lukat-Rodgers, G. S.; Rodgers, K. R.; Benson, D. R. “A Possible Role for the Covalent Heme-Protein Linkage in Cytochrome c Revealed via Comparison of N-Acetylmicroperoxidase-8 and a Synthetic, Monohistidine-Coordinated Heme Peptide” Biochemistry 2004, 43, 1656-1666.
Lushington, G. H.; Cowley, A.B.; Silchenko, S.; Lukat-Rodgers, G. S.; Rodgers, K. R.; Benson, D.R. “Comparison of Thioethers and Sulfoxides as Ligands to N-Acetylmicroperoxidase-8: Implications for Oxidation of Methionine-80 in Cytochrome c” Inorg. Chem. 2003, 42, 7550-7559.
Wang, L.; Urbauer, R. J. B.; Urbauer, J. L.; Benson, D. R. “House Fly Cytochrome b5 Exhibits Kinetically Trapped Hemin and Selectivity in Hemin Binding” Biochem. Biophys. Res. Commun. 2003, 305, 840-845.