Faculty Profiles

Alvin L. Crumbliss
Alvin L. Crumbliss
University Distinguished Service Professor Emeritus
Office: 
2104 French Family Science Center, Box 90346, Durham, NC 27708-0354
Phone: 
(919) 660-1540
alvin.crumbliss@duke.edu
http://sites.duke.edu/crumbliss/
Research Interests: 

Dr. Crumbliss is interested in the function, reactivity and control of transition metals in biological systems. A major emphasis is investigations related to the biochemistry of iron. Through application of in vitro and ex vivo biophysical techniques the Crumbliss group is investigating iron trafficking mediated by proteins and low molecular weight iron carriers (siderophores) in bacterial and mammalian cells. This research is relevant to understanding iron bioavailability, oxidative stress, and the relationship between iron and human health and disease. The redox behavior of various native, mutant and engineered hemoglobins is also under investigation with respect to their role in oxidative stress, signaling and cooperative oxygen transport, and potential application as cell free blood substitutes.

Overview

Education:

Ph.D., Northwestern University 1968

B.A., Knox College 1964

Research Areas:
Biomolecular Structure and Function, Biological, Inorganic

Valdebenito, Marianne, et al. “Environmental factors influence the production of enterobactin, salmochelin, aerobactin, and yersiniabactin in Escherichia coli strain Nissle 1917.” International Journal of Medical Microbiology : Ijmm, vol. 296, no. 8, Dec. 2006, pp. 513–20. Epmc, doi:10.1016/j.ijmm.2006.06.003. Full Text

Mies, Kassy A., et al. “Ternary complex formation facilitates a redox mechanism for iron release from a siderophore.” Biometals : An International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine, vol. 19, no. 2, Apr. 2006, pp. 115–26. Epmc, doi:10.1007/s10534-005-4342-1. Full Text

Chesnut, D. B., and A. L. Crumbliss. “An ELF and AIM study of NO2 and N2O4.” Chemical Physics, vol. 315, no. 1–2, Aug. 2005, pp. 53–58. Scopus, doi:10.1016/j.chemphys.2005.04.002. Full Text

Dhungana, Suraj, et al. “Kinetics of iron release from ferric binding protein (FbpA): mechanistic implications in bacterial periplasm-to-cytosol Fe3+ transport.” Biochemistry, vol. 44, no. 28, July 2005, pp. 9606–18. Epmc, doi:10.1021/bi0505518. Full Text

Summers, Jack S., et al. “Use of phosphorus ligand NMR probes to investigate electronic and second-sphere solvent effects in ligand substitution reactions at manganese(II) and manganese(III).” Inorganic Chemistry, vol. 44, no. 10, May 2005, pp. 3405–11. Epmc, doi:10.1021/ic048618n. Full Text

Dhungana, S., and A. L. Crumbliss. “Coordination chemistry and redox processes in siderophore-mediated iron transport.” Geomicrobiology Journal, vol. 22, no. 3–4, Apr. 2005, pp. 87–98. Scopus, doi:10.1080/01490450590945870. Full Text

Roulhac, Petra L., et al. “SUPREX (Stability of Unpurified Proteins from Rates of H/D Exchange) analysis of the thermodynamics of synergistic anion binding by ferric-binding protein (FbpA), a bacterial transferrin.” Biochemistry, vol. 43, no. 50, Dec. 2004, pp. 15767–74. Epmc, doi:10.1021/bi0481848. Full Text

Bonaventura, Celia, et al. “Critical redox and allosteric aspects of nitric oxide interactions with hemoglobin.” Antioxidants & Redox Signaling, vol. 6, no. 6, Dec. 2004, pp. 979–91. Epmc, doi:10.1089/ars.2004.6.979. Full Text

Bonaventura, C., et al. “New insights into the proton-dependent oxygen affinity of Root effect haemoglobins.” Acta Physiologica Scandinavica, vol. 182, no. 3, Nov. 2004, pp. 245–58. Epmc, doi:10.1111/j.1365-201x.2004.01359.x. Full Text

Dhungana, Suraj, et al. “Phosphate ester hydrolysis is catalyzed by a bacterial transferrin: potential implications for in vivo iron transport mechanisms.” Journal of Inorganic Biochemistry, vol. 98, no. 11, Nov. 2004, pp. 1975–77. Epmc, doi:10.1016/j.jinorgbio.2004.08.004. Full Text

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