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

Batinić-Haberle, I., et al. “Hydrolysis of Ferrioxamine B in Aqueous Micellar Solution.” Inorganic Chemistry, vol. 33, no. 14, July 1994, pp. 3151–58. Scopus, doi:10.1021/ic00092a022. Full Text

Spasojević, I., et al. “Supramolecular Assembly Formation of Ferrioxamine B and Its Al(III), Ga(III), and In(III) Analogues with Dicyclohexano-18-Crown-6 in Chloroform.” Journal of the American Chemical Society, vol. 116, no. 13, June 1994, pp. 5714–21. Scopus, doi:10.1021/ja00092a023. Full Text

Ghio, A. J., et al. “DNA strand breaks following in vitro exposure to asbestos increase with surface-complexed [Fe3+].” Archives of Biochemistry and Biophysics, vol. 311, no. 1, May 1994, pp. 13–18. Epmc, doi:10.1006/abbi.1994.1202. Full Text

Caudle, M. T., et al. “Electrospray Mass Spectrometry Study of 1:1 Ferric Dihydroxamates.” Inorganic Chemistry, vol. 33, no. 5, Mar. 1994, pp. 843–44. Scopus, doi:10.1021/ic00083a001. Full Text

Skelly, J. M., et al. “Formation of Plasma Polymer Thin Films Containing Reactive Metal Chelate Sites.” Chemistry of Materials, vol. 6, no. 2, Feb. 1994, pp. 227–33. Scopus, doi:10.1021/cm00038a022. Full Text

Chaubet, F., et al. “Synthesis and structural studies of new polyhydroxamic iron(III) complexes for the use in nuclear magnetic resonance imaging. Part II: Study of the complexes formed in situ from hydroxamic acids.” Canadian Journal of Chemistry, vol. 72, no. 12, 1994, pp. 2361–68.

Faulkner, K. M., et al. “A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins.” Inorganica Chimica Acta, vol. 226, no. 1–2, Jan. 1994, pp. 187–94. Scopus, doi:10.1016/0020-1693(94)04086-9. Full Text

Skelly, J. M., et al. “Reversible Complexation of O2 to (meso-Tetraphenylporphyrinato)cobalt(II) Plasma Polymer and Sublimed Films at Room Temperature.” Inorganic Chemistry, vol. 32, no. 7, Jan. 1993, pp. 1306–08. Scopus, doi:10.1021/ic00059a046. Full Text

Crumbliss, A. L., et al. “Redox Properties of Phosphazene Polymers with Pendant Ferrocene Groups.” Inorganic Chemistry, vol. 32, no. 26, Jan. 1993, pp. 6088–94. Scopus, doi:10.1021/ic00078a029. Full Text

Crumbliss, A. L., et al. “A carrageenan hydrogel stabilized colloidal gold multi-enzyme biosensor electrode utilizing immobilized horseradish peroxidase and cholesterol oxidase/cholesterol esterase to detect cholesterol in serum and whole blood.” Biosensors & Bioelectronics, vol. 8, no. 6, Jan. 1993, pp. 331–37. Epmc, doi:10.1016/0956-5663(93)85014-f. Full Text

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