Dr. N. DENNIS CHASTEEN

 PROFESSOR OF CHEMISTRY, EMERITIS

BIOPHYSICAL/BIOINORGANIC
MARINE CHEMISTRY

A. B. UNIVERSITY OF MICHIGAN (1962) M. S. UNIVERSITY OF ILLINOIS (1966) PH.D. UNIVERSITY OF ILLINOIS (1969) NIH POSTDOCTRAL FELLOW UNIVERSITY OF COLORADO (1970) FOGARTY SENIOR INTERNATIONAL FELLOW, UNIVERSITY OF BRISTOL, U.K. (1979) FULBRIGHT SENIOR SCHOLAR MURDOCH UNIVERSITY, AUSTRALIA (1989) NIH MERIT AWARDEE (1992 - 2002) Recent Publications Collaborations Instrumentation Methodologies Personnel

Department of Chemistry  Parsons Hall  University of New Hampshire  Durham, NH 03824

Office: (603) 862-2520 Laboratory: (603) 862-1354 Department: (603) 862-1550 Fax: (603) 862-4278 E-mail: ndc@cisunix.unh.edu

INTERESTS: EPR, ESEEM & ENDOR Spectroscopy; metallobiochemistry, radicals in proteins, transition metal chemistry, biomineralization, iron proteins and complexes, vanadium proteins and complexes.

RESEARCH PROGRAM

Our research program is devoted to studies of the bioinorganic and biophysical chemistry of metalloproteins, in particular those proteins involved in the metabolism of iron, i.e. ferritin and transferrin. In addition we have an interest in vanadium biochemistry and in proteins that play a role in shell biomineralization in mollusks. We are also involved in a number of collaborative projects with other faculty at UNH and other universities (see Collaborations).

Ferritin- The ferritins are a class of iron storage proteins found widely distributed among the animal, plant and microbial kingdoms. These proteins consist of 24 subunits assembled into hollow spherical structure within which iron is stored as a hydrous ferric oxide mineral core. Our research focuses on understanding the redox and hydrolysis-mineralization mechanisms by which iron is acquired and released by ferritin. We seek to understand the structural attributes by which this unusual protein is capable of reversibly storing such large quantities of iron (4500 Fe/protein). A variety of spectroscopic, kinetic and thermochemical techniques and site-directed mutagenesis are employed in this research (see Methodologies and Major Instrumentation).

Shell structure of ferritin.*

Ferroxidase site of human ferritin.**

Transferrin - The transferrins are a class of nonheme iron binding proteins primarily found in mammals. They include serum transferrin, ovotransferrin, lactoferrin and melanotransferrin. Serum transferrin, the subject of our research, is a transport protein that carries iron in the circulation to various iron requiring tissues such as bone marrow where it is released for the synthesis of heme proteins. Our work is directed at understanding the spectral, structural and kinetic properties of the protein as they relate to its function in vivo. We collaborate with researchers at the University Vermont on studies of various structurally altered half-molecule transferrins (see Collaborations and Recent Publications).

Bilobal structure of transferrin.*

Iron coordination in transferrin.***

FURTHER INFORMATION

Recent Publications
Collaborations
Instrumentation
Methodologies
Personnel
Consulting

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*Protein structures derived from the protein data base (PDB).
**Adapted from X. Yang, Y. Chen-Barrett, P. Arosio and N. D. Chasteen (1998), Biochemistry 37, 9743.
***Adapted from E. N. Baker (1994), Adv. Inorg. Chem. 41, 389.

Last updated 8/12/2013