N. Dennis Chasteen

N. Dennis Chasteen

Professor Emeritus

Education and Achievements

A.B. 1962, University of Michigan
M.S. 1966, University of Illinois
Ph.D. 1969, University of Illinois
NIH Postdoctoral Fellow, 1970, University of Colorado
Fogarty Senior International Fellow, 1979, University of Bristol, U.K.
Fulbright Senior Scholar, 1989, Murdoch University, Australia
NIH Merit Awardee, 1992-2002

Interests

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

Research

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.
 

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.

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.

       

Collaborations

We collaborate with researchers in the United States and abroad on a number of different research projects of mutual interest.

Prof. Anne B. Mason, Department of Biochemistry, University of Vermont: Electron resonance studies of site directed mutants of the N terminal and C-terminal half molecules of human serum transferrin and their interaction with the receptor.

Prof. Paolo Arosio, University of Brescia, Milan: Spectroscopic, kinetic and thermodynamic studies of site directed variants of recombinant human ferritins.

Prof. Fadi Bou-Abdallah, Department of Chemistry, State University of New York – Potsdam:  Structure-function relationships in ferritins.

 

Recent Publications

101. "Ferritin. Uptake, Storage and Release of Iron", N. D. Chasteen in Metal Ions in Biological Systems", Vol. 35 (H. Sigel and A. Sigel, eds.), Marcel Dekker, Inc., New York, 1998, pp 479 - 514.

102. "Mutations of Nonliganding Residues Tyr-85 and Glu-83 in the N-Lobe of Human Serum Transferrin. Functional Second Shell Effects", Q.-Y. He, A. B. Mason, R. C. Woodworth, B. M. Tam, R. T. A. MacGillivray, J. K. Grady, and N. D. Chasteen, J. Biol. Chem. 273, 17018 (1998).

103. "Reaction Paths of Iron Oxidation and Hydrolysis in Horse Spleen and Recombinant Human Ferritins", X. Yang, Y. Chen-Barrett, P. Arosio and N. D. Chasteen, Biochemistry 37, 9743-9750 (1998). http://pubs.acs.org/cgi-bin/download.pl?bi973128a/45iL

104. "X-Band EPR Studies of Ferroelectric Lead Titanate (PT, and Piezoelectric Lead magnesium Niobate (PMN) and PMN/PT Powders at 10 K and 85 K", J. Huang, N. D. Chasteen and J. J. Fitzgerald, Chem. Mater., 10, 3848-3855 (1999).

105. "Ferroxidase Activity of Ferritin, Effects of pH, Buffer, Fe(II) and Fe(III) Concentrations" X. Yang and N. D. Chasteen, Biochem. J. 338, 615-618 (1999).

106. "Mineralization in Ferritin: An Efficient Means of Iron Storage", N. D. Chasteen and P. M. Harrison, J. Struct. Biol. 126,  182-194 (1999).

107. "A New Robust Coupler for the Q-band Cylindrical TE011Cavity", J. Shao and N. D. Chasteen, EPR Newsletter, 9, 10 (1999).

108.  "Preparation and Use of a Magnetic Field Set and Sweep Standard", N. D. Chasteen, J. K. Grady and J. Shao, EPR Newsletter 10, No 4, 7-9 (1999).

109. "Molecular Diffusion into Ferritin. Pathways, Temperature Dependence, Incubation Time and Concentration Effects", X. Yang, P. Arosio, and N. D. Chasteen, Biophys. J. 78, 2049-2059 (2000).

110. "Mutations at the Histidine 249 Ligand Profoundly Alter the Spectral and Iron-Binding Properties of Human Serum Transferrin N-Lobe", Q.-Y. He, A. B. Mason, R. Pakdaman, N. D. Chasteen, B. K. Dixon, B. M. Tam, V. Nguyen, R. T. A. MacGillivray and R. C. Woodworth, Biochemistry, 39, 1205-1210 (2000).

111. "Vanadyl(IV) Binding to Mammalian Ferritins.  An EPR Study Aided by Site-Directed Mutagenesis", J. K. Grady, J. Shao, P. Arosio, P. Santambrogio and N. D. Chasteen,  J. Inorg. Biochem. 80, 107-113 (2000).

112. "ESEEM and ENDOR Spectroscopy", N. D. Chasteen and P. A. Snetsinger in Physical Methods in Bioinorganic Chemistry: Spectroscopy and Magnetism (L. Que, Jr., ed.), University Science Books, Sausalito, CA, 2000, pp 187-231.

113. "Improvements in Dating Tooth Enamel by ESR", A. R. Skinner, B. A. B. Blackwell, N. D. Chasteen,  J. Shao, and S. S. Min, Appl. Rad. Iso. 52, 1337-1344 (2000).

114. "The Iron Oxidation and Hydrolysis Chemistry of Escherichia coli Bacterioferritin", X. Yang, N. E. Le Brun, A. J. Thomson, G. R. Moore and N. D. Chasteen, Biochemistry 39, 4915-4923 (2000). http://pubs.acs.org/cgi-bin/download.pl?bi992631f/e2gY.

115. "Iron Oxidation and Hydrolysis reactions of Novel Ferritin from Listeria innocua", X. Yang, E. Chiancone, S. Stefanini, A. Ilari and N. D. Chasteen, Biochem. J. 349, 783-786 (2000).

116. "Q-band Studies of the ESR Signal in Tooth Enamel", A. R. Skinner, N. D. Chasteen, J. Shao, and B. A. B. Blackwell, Quaternary Geochronology 2020, 1027-1030 (2001).

117.  "Purification and Characterization of  Novel Calcium Binding Protein from the Extrapallial Fluid of the Mollusc, Mytilus edulis", S. J. Hattan, T. M. Laue, and N. D. Chasteen, J. Biol Chem. 276, 4461-4468 (2001).

118. "Copper Complexes of Novel N-Alkylated Derivatives of cis,cis-1,3,5-Triaminocyclohexane. 1. Preparation and Structure", G. Park, J. Shao, F. H. Lu, R. D. Rogers, N. D. Chasteen, M. W. Brechbiel and R.P. Planalp, Inorg. Chem. 40, 4176-4182 (2001).

119. "Copper Complexes of Novel N-Alkylated Derivatives of cis,cis-1,3,5-Triaminocyclohexane. 2. Metal-Promoted Phosphate Diester hydrolysis", K. A. Deal, G. Park, J. Shao,  N. D. Chasteen, M. W. Brechbiel and R.P. Planalp, Inorg. Chem. 40, 4176-4182 (2001).

120. "Is Hydrogen Peroxide Produced during Iron(II) Oxidation in Mammalian Apoferritins?", G. Zhao, F. Bou-Abdallah, X. Yang, P. Arosio and N. D. Chasteen, Biochemistry 40, 10832-10838 (2001). http://pubs.acs.org/cgi-bin/download.pl?bi011052j/q2MN

121. "Characterization of the H- and L-Subunit Ratios of Ferritins by Sodium Dodecyl Sulfate-Capillary Gel Electrophoresis", J. K. Grady, J. Zang, T. M. Laue, P. Arosio and N. D. Chasteen, Anal. Biochem. 302, 263-268 (2002).

122. "Deuterium Structural Effects in Inorganic and Bioinorganic Aggregates", J. Lee, N. D. Chasteen, G. Zhao, G. C. Papaefthyiou, and S. M. Gorun, J. Am. Chem. Soc. 124, 3042-3049 (2002).

123. "Mu-1,2-Peroxobridged Di-Iron(III) Dimer Formation in Human H-Chain Ferritin", F. Bou-Abdallah, G. C. Papaefthymiou, D. M. Scheswohl, S. D. Stanga, P. Arosio and N. D. Chasteen, Biochem. J., 364, 57-63 (2002).

124.  "Iron and Hydrogen Peroxide Detoxification Properties of DNA-binding Protein from Starved Cells. A Ferritin-Like DNA-Binding Protein of Escherichia Coli", G. Zhao, P. Ceci, A. Ilari, L. Giangiacomo, T. M. Laue, E. Chiancone, and N. D. Chasteen,  J. Biol. Chem. 277 27689-27696 (2002).

125. "Ferrous Ion Binding to Recombinant Human H-Chain Ferritin.  An Isothermal Titration Calorimetry Study", F. Bou-Abdallah, P. Arosio, P. Santambrogio, X. Yang, C. Janus-Chandler and N. D. Chasteen,  Biochemistry 41, 11184-11191 (2002). http://pubs.acs.org/cgi-bin/download.pl?bi020215g/o7Pw

126. "Iron Detoxification Properties of Escherichia coli Bacterioferritin. Attentuation of Oxyradical Chemistry", F. Bou-Abdallah, A. C. Lewin, N. E. Le Brun, G. R. Moore, and N. D. Chasteen, J. Biol. Chem. 277 37064-37069 (2002).

127. "Multiple Pathways for Mineral Core Formation in Mammalian Apoferritin. The Role of Hydrogen Peroxide", G. Zhao, F. Bou-Abdallah, P. Arosio, S. Levi, C. Janus-Chandler, and N. D. Chasteen, Biochemistry 42, 3142-3150 (2003). http://pubs.acs.org/cgi-bin/download.pl?bi027357v/Q8ky

128. "Defining Metal Ion Inhibitor Interactions with Recombinant Human H- and L-chain ferritins and Site-Directed Variants: An Isothermal Titration Calorimetry Study", F. Bou-Abdallah, P. Arosio, S. Levi, C. Janus-Chandler and N. D. Chasteen, J. Biol. Inorg. Chem. 8, 489-497 (2003).

129. "Anion Exchange in Human Serum Transferrin N-Lobe: A Model Study with Variant His249Ala, Q.-Y. He, R. C. Woodworth and N. D. Chasteen, J. Biol. Inorg. Chem. 8, 635-643 (2003).

130. "The Putative Nucleation Site in Human H-chain ferritin is not Required for Mineralization of the Iron Core", F. Bou-Abdallah, P. Arosio and N. D. Chasteen, Biochemistry 43, 4332-4337 (2004). http://pubs.acs.org/cgi-bin/download.pl?bi0498813/o6Xf

131. "Iron Binding and Oxidation Kinetics in Frataxin CyaY of Escherichia coli", F. Bou-Abdallah, S. Adinolfi, A. Pastore, T. M. Laue and N. D. Chasteen J. Mol. Biol. 341, 605-615 (2004)

132.  “Unique Iron Binding and Oxidation Properties of Human Mitochondrial Ferritin.  A Comparative Analysis with Human H-Chain Ferritin”  F. Bou-Abdallah, P. Santambrogio, S. Levi, P. Arosio, and N. D. Chasteen, J. Mol. Biol. 347, 543-554 (2005).

133. “Origin of the Unusual Kinetics of Iron Deposition in Human H-Chain Ferritin” F. Bou-Abdallah, G. Zhao, H. R. Mayne, P.Arosio and N. D. Chasteen, J. Am. Chem. Soc.  127, 3885-3893 (2005). http://pubs.acs.org/cgi-bin/download.pl?ja044355k/Q5pz

134. “The So-Called Listeria innocua Ferritin is a Dps Protein. Iron Incorporation, Detoxification and DNA Protection Properties” M. Su, S. Cavallo, S. Stefanini, E. Chiancone and N. D. Chasteen,  Biochemistry 44, 5572-5578 (2005). http://pubs.acs.org/cgi-bin/download.pl?bi0472705/b5Zg

135. “The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification, but not for iron uptake. A study with site-specific mutants” A. Ilari, M. C. Latella, P. Ceci, F. Ribacchi, M. Su, L. Giangiacomo, S. Stefanini, N. D. Chasteen, and E. Chiancone, Biochemistry 44, 5579-5587 (2005). http://pubs.acs.org/cgi-bin/download.pl?bi050005e/A4W2

136. “Mutational Analysis of C-lobe Ligands of Human Serum Transferrin: Insights into the Mechanism of Iron Release”, Anne B. Mason, Peter J. Halbrooks, Nicholas G. James,  Susan A.Connolly, Julia R. Larouche, Valerie C. Smith, Ross T.A. MacGillivray and N. Dennis Chasteen, Biochemistry 44, 8013-8021 (2005). http://pubs.acs.org/cgi-bin/download.pl?bi050015f/J5ov

137. “Structural Characterization of the Major Extrapallial Fluid Protein of the Mollusc Mytilus edulis: Implications for Function” Y. Yin, J. Huang, M. L. Paine, V. N. Reinhold and N. D. Chasteen, Biochemistry 44, 10720-10731 (2005). http://pubs.acs.org/cgi-bin/download.pl?bi0505565/s8Kb

138. “Mu-1,2-Peroxo Diferric Complex Formation in Horse Spleen Ferritin. A Mixed H/L-Subunit Heteropolymer” G. Zhao, M. Su and N. D. Chasteen, J. Mol. Biol. 352, 467-477 (2005).

139. “Thermodynamic Analysis of Ferrous Ion Binding to Escherichia coli Ferritin EcFtnA” F. Bou Abdallah, M. R. Woodhall, A. Velesquez-Campoy, S. C. Andrews and N. D. Chasteen, Biochemistry 44, 13837-13846 (2005).

140. “Oxidation of Good’s Buffers by Hydrogen Peroxide” G. Zhao and N. D. Chasteen Analyt. Biochem. 349, 262-267 (2006).

141. “Iron(II) and Hydrogen Peroxide Detoxification Properties of Human H-Chain Ferritin”. An EPR Spin-Trapping Study”, G. Zhao, P. Arosio and N. D. Chasteen, Biochemistry 45, 3429-3436 (2006).

142. “Quenching of Superoxide Radicals by Green Fluorescent Protein”, F. Bou-Abdallah, N. D. Chasteen and M. P. Lesser, Biochim. Biophys. Acta 1760, 1690-1695 (2006).

143. “Deuterium Isotope Effects on Iron Core Formation in Ferritin”, G. C. Papaefthymiou, A. J. Viescas, R. Horn, E. Carney, G. Zhao, N. D. Chasteen, J. Lee and S. M. Gorun, Hyperfine Interactions 165, (1-4), 333-338 (2006) DOI: 10.1007/s10751-006-9280-y.

144. “A Comparative Mossbauer Study of the Mineral Cores of Human H-ferritin employing Dioxygen and Hydrogen Peroxide as Oxidants.’ F. Bou-Abdallah, E. Carney, N. D. Chasteen, P. Arosio, A. Viescas and G. Papaefthymiou, Biophys. Chem. 130, 114-121 (2007).

145. “Iron-Binding Properties of Plant Phenolics and Cranberry’s Bio-effects” M. Guo, C. Perez, Y. Wei, E. Rapoza, G. Su, F. Bou-Abdallah and N. D. Chasteen, J. Chem. Soc. Dalton 4951-4961 (2007) DOI: 10.1039/b705136k, http://www.rsc.org/ej/dt/preprints/10/DD10/b705136k.pdf

146. “Spin Concentration Measurements of High-Spin (g ′ = 4.3) Rhombic Iron(III) ions in Biological Samples: Theory and Application” F. Bou-Abdallah and N. D. Chasteen, J. Biol. Inorg. Chem. 13, 15-24 (2007) DOI 10.1007/s00775-007-0304-0.

147. “The salty science of the aluminum-air battery” S. V. Chasteen, N. D. Chasteen, and P. Doherty, The Physics Teacher, 544-547 (2008).

148. “Facilitated Diffusion of Iron(II) and Dioxygen Substrates Into Human H-Chain Ferritin.  A Fluorescence and Absorbance Study Employing the Ferroxidase Center Substitution Y34W” F. Bou-Abdallah, G. Zhao, G. Biasiotto, M. Poli, P. Arosio and N. D. Chasteen, J. Am. Chem. Soc. 130, 17801–17811 (2008) DOI: 10.1021/ja8054035

149. “Protein Association and Dissociation Regulated by Ferric Ion: A Novel Pathway for Oxidative Deposition of Iron in Pea Seed Ferritin” C. Li, X. Fu, X. Qi, X. Hu, N. D. Chasteen and G. Zhao,
J. Biol. Chem. 284, 16743 - 16751 (2009) DOI:10.1074/jbc.M109.011528

150. “Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin” A. B. Mason, P. J. Halbrooks, N. G. James, S. L. Byrne, J. K. Grady, N. D. Chasteen, C. E. Bobst, I. A. Kaltashov, V. C. Smith, R. T. A. MacGillivray and S. J. Everse, Biochemistry 48, 1945–1953 (2009) DOI: 10.1021/bi802254x

151. “A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping”, A. B. Mason, S. L. Byrne, S. J. Everse, S. E. Roberts, N. D. Chasteen, V. C. Smith, R. T. A. MacGillivray, B. Kandemir and F. Bou-Abdallah, J. Mol. Recogn. 22, 521-529 (2009).

152. “Hyperfine and quadrupolar interactions in vanadyl protein and model complexes. Theory and Experiment”, S. Larsen and N. D. Chasteen in Applications of high resolution EPR to metalloproteins . Biological Magnetic Resonance, Vol. 29, (G. R. Hanson and L. J. Berliner, eds.), Springer, New York, 2010, pp 372–410.

153. “The Unique Kinetics of Iron Release from Transferrin: The Role of Receptor, Lobe-Lobe Interactions, and Salt at Endosomal pH”, S. L. Byrne, N. D. Chasteen, A. N. Steere and A. B. Mason, J. Mol. Biol. 396, 130-140 (2010).

154. “Identification of a Kinetically Significant Anion Binding (KISAB) Site in the N-Lobe of Human Serum Transferrin”, S. L. Byrne, A. N. Steere, N. D. Chasteen and A. B. Mason, Biochemistry 49 4200-4207 (2010).

155. “The sedimentation properties of ferritins. New insights and analysis of methods of nanoparticle preparation”, C. A. May, Grady, J. K., Laue, T. M., Poli, M., Arosio, P., and Chasteen, N. D., Biochim. Biophys. Acta, General Subjects 1800(8), 858-87 (2010).

156. “Dedication to Pauline M. Harrison”, Chasteen, N. D., Biochim. Biophys. Acta, General Subjects 1800(8), 689-690 (2010).

157. “Evidence that His349 acts as a pH-inducible switch to accelerate receptor-mediated iron release from the C-lobe of human transferrin”, Steere, A. N., Byrne, S. L., Chasteen, N. D., Smith, V. C., MacGillivray, R. T. A., and Mason, A. B. , JBIC, 15(8), 1341-1352 (2010).

158. “How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH”, Eckenroth, B. E., Steere, A. N., Chasteen, N. D., Everse, S. J., Mason, A. B., PNAS (USA) 108(32), 13089-13094 (2011).

159. “Ionic residues of human serum transferrin affect binding to the transferrin receptor and iron release”, Steere, A. N., Miller, B. F., Roberts, S. E., Byrne, S. L., Chasteen, N. D., Smith Valerie, Macgillivray, R. T. A., Mason, A. B., Biochemistry 51, 686-694 (2012).

160. “Kinetics of iron release from transferrin bound to the transferrin receptor at endosomal pH, Steere, A. N. Byrne, S. L., Chasteen N. D., Mason A. B. Biochim. Biophys. Acta, General Subjects, 1820, 326-333 (2012).

161. “Structure-based mutagenesis reveals critical residues in the transferrin receptor participating in the mechanism of pH-induced release of iron from human serum transferrin”, Steere, A. N., Chasteen, N. D., Miller, B. F., Smith, V. C., Macgillivray, R. T. A., Mason, A. B., Biochemistry 51, 2113-2121 (2012).

162. “Dedication to Philip Aisen”, Chasteen, N. D., Biochim. Biophys. Acta, General Subjects (2012) 1820, 159-160.

163. “Anomalous N-glycan structures with an internal fucose branched to GlcA and GlcN residues isolated from a mollusk shell-forming fluid”, Zhou, H., Hanneman, A. J., Chasteen, N. D., Reinhold, V. N., J. Proteome Research (2013) 12, 4557-4555.  

164. “Functionality of the Three-Site Ferroxidase Center of Escherichia coli Bacterial Ferritin (EcFtnA)”, Bou-Abdallah, F., Yang, H. Awomolo, A., Cooper, B., Woodhall, M. R., Andrews, S.C., Chasteen, N. D., Biochemistry (2014) 53, 483-495.

165. “Exploring the Fe(III) binding sites of human serum transferrin with EPR at 275 GHz”, Mathies, G., Gast, P., Chasteen, N. D., Luck, A. N., Mason, A. B., Groenen, J.J., J. Biol. Inorg. Chem. (2015) 20, 487-496.

 
Updated 6/21/2016

 
 
 

 

 

Portrait of Dennis Chasteen
Department of Chemistry
23 Academic Way
Durham, NH 03824
Fax: 
603-862-4278