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

Dhungana, Suraj, et al. “Iron chelation properties of an extracellular siderophore exochelin MS.” Inorganic Chemistry, vol. 43, no. 20, Oct. 2004, pp. 6274–83. Epmc, doi:10.1021/ic049343e. Full Text

Heymann, J. J., and A. L. Crumbliss. “Kinetics and mechanism of axial ligand substitution of alkyl cobaloximes by substituted pyridines in different solvents.” Chemtracts, vol. 17, no. 10, Oct. 2004, pp. 527–33.

Gabricević, Mario, et al. “Kinetics and mechanism of iron(III) complexation by ferric binding protein: the role of phosphate.” Biochemistry, vol. 43, no. 19, May 2004, pp. 5811–19. Epmc, doi:10.1021/bi036217y. Full Text

Boukhalfa, Hakim, et al. “Beryllium(II) binding to ATP and ADP: potentiometric determination of the thermodynamic constants and implications for in vivo toxicity.” Biometals : An International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine, vol. 17, no. 2, Apr. 2004, pp. 105–09. Epmc, doi:10.1023/b:biom.0000018359.25658.9c. Full Text

Dhungana, Suraj, et al. “Redox properties of human transferrin bound to its receptor.” Biochemistry, vol. 43, no. 1, Jan. 2004, pp. 205–09. Epmc, doi:10.1021/bi0353631. Full Text

Dhungana, Suraj, et al. “Crystal and molecular structures of ionophore-siderophore host-guest supramolecular assemblies relevant to molecular recognition.” Journal of the American Chemical Society, vol. 125, no. 48, Dec. 2003, pp. 14760–67. Epmc, doi:10.1021/ja035778+. Full Text

Boukhalfa, Hakim, et al. “Kinetics and mechanism of iron release from the bacterial ferric binding protein nFbp: exogenous anion influence and comparison with mammalian transferrin.” Journal of Biological Inorganic Chemistry : Jbic : A Publication of the Society of Biological Inorganic Chemistry, vol. 8, no. 8, Nov. 2003, pp. 881–92. Epmc, doi:10.1007/s00775-003-0487-y. Full Text

Weaver, K. D., and A. L. Crumbliss. “High-Resolution Structure of an Alternate Form of the Ferric Ion Binding Protein from Haemophilus influenzae.” Chemtracts, vol. 16, no. 12, Nov. 2003, pp. 715–21.

Fago, Angela, et al. “The case of the missing NO-hemoglobin: spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry.” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 21, Oct. 2003, pp. 12087–92. Epmc, doi:10.1073/pnas.2032603100. Full Text

Wirgau, J. I., and A. L. Crumbliss. “Carrier-facilitated bulk liquid membrane transport of iron(iii) hydroxamate complexes utilizing a labile recognition agent and amine recognition in the second coordination sphere.” Journal of the Chemical Society. Dalton Transactions, vol. 3, no. 19, Sept. 2003, pp. 3680–85. Scopus, doi:10.1039/b306810b. Full Text

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