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

Taboy, C. H., et al. “Fe3+ coordination and redox properties of a bacterial transferrin.” The Journal of Biological Chemistry, vol. 276, no. 4, Jan. 2001, pp. 2719–24. Epmc, doi:10.1074/jbc.m004763200. Full Text

Spasojević, I., et al. “Aqueous solution speciation of Fe(III) complexes with dihydroxamate siderophores alcaligin and rhodotorulic acid and synthetic analogues using electrospray ionization mass spectrometry.” Inorg Chem, vol. 40, no. 1, Jan. 2001, pp. 49–58. Pubmed, doi:10.1021/ic991390x. Full Text

Summers, J. S., et al. “Enhancement of the 1H and 31P NMR Resonances of Methylphosphite and Methylethylphosphate Anions by Selected Metal Complexes.” Inorg. Chem., vol. 40, 2001.

Taboy, C. H., et al. “Concentration-dependent effects of anions on the anaerobic oxidation of hemoglobin and myoglobin.” The Journal of Biological Chemistry, vol. 275, no. 50, Dec. 2000, pp. 39048–54. Epmc, doi:10.1074/jbc.m004547200. Full Text

Boukhalfa, H., et al. “Kinetics and mechanism of iron(III) dissociation from the dihydroxamate siderophores alcaligin and rhodotorulic acid.” Inorganic Chemistry, vol. 39, no. 25, Dec. 2000, pp. 5591–602. Epmc, doi:10.1021/ic000330k. Full Text

Dhungana, S., and A. L. Crumbliss. “Mutations at the histidine 249 ligand profoundly alter the spectral and iron-binding properties of human serum transferrin N-lobe: Mutation of the iron ligand His 249 to Glu in the N-lobe of human transferrin abolishes the dilysine "Trigger" but does not significantly affect iron release.” Chemtracts, vol. 13, no. 12, Dec. 2000, pp. 770–75.

Gupta, A., and A. L. Crumbliss. “Treatment of iron deficiency anemia: are monomeric iron compounds suitable for parenteral administration?” The Journal of Laboratory and Clinical Medicine, vol. 136, no. 5, Nov. 2000, pp. 371–78. Epmc, doi:10.1067/mlc.2000.110368. Full Text

Boukhalfa, H., and A. L. Crumbliss. “Multiple-path dissociation mechanism for mono- and dinuclear tris(hydroxamato)iron(III) complexes with dihydroxamic acid ligands in aqueous solution.” Inorganic Chemistry, vol. 39, no. 19, Sept. 2000, pp. 4318–31. Epmc, doi:10.1021/ic0001659. Full Text

Trzaska, S. M., et al. “Microcalorimetric determination of thermodynamic parameters for ionophore-siderophore host-guest complex formation.” Inorganic Chemistry, vol. 39, no. 6, Mar. 2000, pp. 1071–75. Epmc, doi:10.1021/ic9908571. Full Text

Spasojevic, Ivan, et al. “Electrochemical Behavior of the Fe(III) Complexes of the Cyclic Hydroxamate Siderophores Alcaligin and Desferrioxamine E.” Inorg Chem, vol. 38, no. 3, Feb. 1999, pp. 449–54. Pubmed, doi:10.1021/ic980635n. Full Text

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