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

Albrecht-Gary, A. M., and A. L. Crumbliss. “Coordination chemistry of siderophores: thermodynamics and kinetics of iron chelation and release.” Metal Ions in Biological Systems, vol. 35, Jan. 1998, pp. 239–327.

Bonaventura, C., et al. “Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and Deer Lodge beta2(NA2)His --> Arg.” Biochemistry, vol. 37, no. 2, Jan. 1998, pp. 496–506. Epmc, doi:10.1021/bi971574s. Full Text

Crumbliss, A. L. “Preorganization of ferric alcaligin, Fe 2L 3. The first structure of a ferric dihydroxamate siderophore.” Chemtracts, vol. 10, no. 5, Dec. 1997, pp. 354–58.

Batinić-Haberle, I., et al. “Solvent effect on second-sphere coordination of ferrioxamine B with substituted 18-crown-6 and 30-crown-10 crown ethers in dichloromethane as compared to chloroform.” Inorganica Chimica Acta, vol. 260, no. 1, July 1997, pp. 35–41. Scopus, doi:10.1016/S0020-1693(96)05528-4. Full Text

Ghio, A. J., et al. “Hypothesis: iron chelation plays a vital role in neutrophilic inflammation.” Biometals, vol. 10, no. 2, Apr. 1997, pp. 135–42. Pubmed, doi:10.1023/a:1018387308517. Full Text

Zhao, J., et al. “Mediator-free amperometric determination of toxic substances based on their inhibition of immobilized horseradish peroxidase.” Biotechnology Progress, vol. 12, no. 5, Sept. 1996, pp. 703–08. Epmc, doi:10.1021/bp960056q. Full Text

Batinic-Haberle, Ines, et al. “Second-Sphere Coordination of Ferrioxamine B and Association of Deferriferrioxamine B, CH(3)(CH(2))(4)NH(3)(+), NH(4)(+), K(+), and Mg(2+) with Synthetic Crown Ethers and the Natural Ionophores Valinomycin and Nonactin in Chloroform.” Inorg Chem, vol. 35, no. 8, Apr. 1996, pp. 2352–59. Pubmed, doi:10.1021/ic951414+. Full Text

Crumbliss, A. L., et al. “Molecular recognition of stable metal complexes through second-sphere coordination by macrocycles.” Pure and Applied Chemistry, vol. 68, no. 6, Jan. 1996, pp. 1225–30. Scopus, doi:10.1351/pac199668061225. Full Text

Batinic-Haberle, I., et al. “Second-Sphere Coordination of Ferrioxamine B and Association of Deferriferrioxamine B, CH3(CH2)4NH3+, NH4+, K+, and Mg2+ with Synthetic Crown Ethers and the Natural lonophores Valinomycin and Nonactin in Chloroform.” Inorganic Chemistry, vol. 35, no. 8, 1996, pp. 2352–59.

Zhao, J., et al. “A xanthine oxidase/colloidal gold enzyme electrode for amperometric biosensor applications.” Biosensors and Bioelectronics, vol. 11, no. 5, Jan. 1996, pp. 493–502. Scopus, doi:10.1016/0956-5663(96)86786-8. Full Text

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