Marquee Middle Image

Faculty Profile

Denis L. Rousseau, Ph.D.

Dr. Denis L. Rousseau

Professor, Department of Physiology & Biophysics

Chair, Department of Physiology & Biophysics

 

Professional Interests

In our laboratory the mechanisms and properties of two enzymes, cytochrome c oxidase and nitric oxide synthase, are being investigated as well as the molecular basis of protein folding. Cytochrome c oxidase is the terminal enzyme in the electron transfer chain. Physiologically, it reduces oxygen to water and utilizes the excess energy to translocate protons across the mitochondrial membrane. The enzyme is responsible for over 90% of the oxygen consumption by living organisms in the biosphere; yet the mechanism of its basic function, the coupling between the redox processes and proton translocation is undetermined. Our objective is to obtain a quantitative description of the manner by which oxygen is reduced to water by exploiting laser spectroscopic methods and rapid mixing techniques developed in our laboratory. These studies will allow us to identify all of the intermediates in the catalytic reaction and thereby establish the molecular basis for one of the most important processes in bioenergetics. Nitric oxide has been found to play many diverse physiological roles ranging from a neurotransmitter, a vasodilator and a cytotoxic agent. The enzyme that catalyzes the formation of NO from oxygen and arginine is nitric oxide synthase, a very complex enzyme containing several cofactors and a heme group which is part of the catalytic site. We have discovered that NO the enzymatic product, inhibits the enzyme and are now studying the mechanism of the inhibition process. In addition, we are studying a variety of inhibitors of the enzyme to sort between the many mechanisms of inhibition that are possible in nitric oxide synthase. These studies will serve as a foundation for the development of drugs that can be used to treat many different syndromes associated with the under- or over-production of NO. How a protein folds into its three dimensional structure is one of the central questions in molecular biology and in the biotechnology industry. To advance the understanding of protein folding, it is necessary to determine the structures and the kinetics of the intermediates in the folding pathway. For this, we developed submillisecond mixers in which folding can be initiated in less than 100 microseconds, a time scale that is over an order of magnitude faster than previously possible. This already has allowed us to discover a new model that accounts for the folding of cytochrome c from 100 microseconds to the formation of the native state. Many new experiments with several different techniques will be done to test the generality of this model and its possible role in other proteins.
 

Selected Publications

204. Regulation of the monomer-dimer equilibrium in inducible nitric oxide synthase by NO D. Li, E. Y. Hayden, K. Panda, D. J. Stuehr, H. Deng, D. L. Rousseau & S.-R Yeh. J. Biol. Chem., Jan 2006; doi:10.1074/jbc.M507328200 203. Structural Characterization of the PCO/O2 Compound of Cytochrome c Oxidase H. Ji, S.-R. Yeh & D. L. Rousseau FEBS Letters 579, 6361-6364 (2005). 202. Ligand-protein interactions in nitric oxide synthase. D. L. Rousseau, David Li, Manon Couture & Syun-Ru Yeh J. Inorg. Biochem., 99, 306-323 (2005). 200. Modulation of the folding energy landscape of cytochrome c with salt. Shi Zhong, Denis L. Rousseau & Syun-Ru Yeh. J. Am. Chem. Soc. 126, 13934-13935 (2004). 199. Heme distortion modulated by ligand-protein interactions in inducible nitric-oxide synthase D. Li, D. J. Stuehr, S.-R. Yeh & D. L. Rousseau J. Biol. Chem. 279, 26489-26499 (2004). 198. Crystal Structure of the Dioxygen-bound Heme Oxygenase from Corynebacterium diphtheriae: Implications for Heme Oxygenase function. M. Unno, T. Matsui, G. C. Chu, M. Couture, T. Yoshida, D. L. Rousseau, J. S. Olson & M. Ikeda-Saito J. Biol. Chem., 279, 21055-21061 (2004). 197. Distal Heme pocket Conformers of Carbonmonoxy Derivatives of Ascaris Hemoglobin: Evidence of Conformational Trapping in Porous Sol-Gel Matrices. T. K. Das, U. Samuni, Y. Lin, D. E. Goldberg, D. L. Rousseau & J. M. Friedman Biochemistry, J. Biol. Chem. 279, 21055-61 (2004). 196. Active site structure of the aa3 quinol oxidase of Acidianus ambivalens. T. K. Das, C. M. Gomes, T. M. Bandeiras, M. M. Pereira, M. Teixeira & D. L. Rousseau Biochem. Biophys. Acta Bioenergetics, Biochem. Biophys. Acta 1655, 306-20 (2004). 195. Elucidation of the Atheriosclerotic Disease Process in apo-E and Wild Type Mice by Vibrational Spectroscopy. F. Adar, L. Jelicks, C. Naudin, D. L. Rousseau & S.-R. Yeh SPIE 5321A-11 (2004). 194. Modulation of the electron redistribution in mixed valence cytochrome c oxidase by protein conformational changes. H. Ji, S.-R. Yeh & D. L. Rousseau J. Biol. Chem. 279, 9392-9399 (2004) 193. Ultrafast microfluidic mixer and freeze-quenching device. Y. Lin, G. J. Gerfen, D. L. Rousseau & S.-R. Yeh Anal. Chem. 75, 5381-5386 (2003). 192. Time-Resolved Resonance Raman Spectroscopy of Intermediates in Cytochrome Oxidase. D. L. Rousseau & S. Han Methods in Enzymology 354, 351-368 (2002). 191. Ca2+-Binding Site in Rhodobacter Sphaeroides Cytochrome c Oxidase. A. Lee, A. Kirichenko, T. Vygodina, S. A. Siletsky, T. K. Das, D. L. Rousseau, R. Gennis & A. A. Konstantinov. Biochemistry 41, 8886-8898 (2002). 190. The Intestinal Fatty Acid Binding Protein: The Role of Turns in Fast and Slow Folding Processes. K. Chattopadhyay, S. Zhong, S.-R. Yeh, D. L. Rousseau & C. Frieden Biochemistry 41, 4040-4047 (2002). 189. Regulation of the Properties of the Heme-NO Complexes in Nitric Oxide Synthase by Hydrogen Bonding to the Proximal Histidine. M. Couture, S. Adak, D. J. Stuehr & D. L. Rousseau J. Biol. Chem. 276, 38280-38288 (2001). 188. The Heme Environment of Mouse Neuroglobin. Evidence for the Presence of Two Conformations of the Heme Pocket. M. Couture, T. Burmester, T. Hankeln & D. L. Rousseau J. Biol. Chem. 276, 36377-36382 (2001). 187. Binding of NO and CO to the d1 Heme of the cd1 Nitrite Reductase. T. K. Das, E. K. Wilson, F. Cutruzzola, M. Brunori & D. L. Rousseau Biochemistry 40, 10774-10781 (2001). 186. Axial Ligation States of Five-Coordinate Heme Oxygenase Proximal Histidine Mutants, as Revealed by EPR and Resonance Raman Spectroscopy. G. C. Chu, M. Couture, T. Yoshida, D. L. Rousseau, & M. Ikeda-Saito J. Am. Chem. Soc. 122, 12612-12613 (2000). 185. Hierarchical Folding of Intestinal Fatty Acid Binding Protein. S.-R. Yeh, I. J. Ropson & D. L. Rousseau Biochemistry 40, 4205-4210 (2001). 184. Simultaneous Observation of the O-O and the Fe-O2 Stretching Modes in Oxyhemoglobins. T. K. Das, M. Couture, Y. Ouellet, M. Guertin & D. L. Rousseau Proc. Nat. Acad. Sci. USA 98, 479-484 (2001). 183. Ligand Binding in the Ferric and Ferrous States of Paramecium Hemoglobin. T. K. Das, R. E. Weber, S. Dewilde, J. B. Wittenberg, B. A. Wittenberg, K. Yamauchi, M. L. Van Hauwaert, L. Moens & D. L. Rousseau Biochemistry 39, 14330-14340 (2000). 182. Design and Implementation of a Rapid-Mixer Flow-Cell for Time Resolved Infrared Microspectroscopy. Marinkovic, A. R. Adzic, M. Sullivan, K. Kovacs, L. M. Miller, D. L. Rousseau, S.-R. Yeh & M. R. Chance Rev. Sci. Instrum. 71, 4057-4060 (2000). 181. Structural Investigations of the Hemoglobin of the Cyanobacterium Synechocystis PCC6803 Reveal a Unique Distal Heme Pocket. M. Couture, T. K. Das, P.-Y. Savard, Y. Ouellet, J. B. Wittenberg, B. A. Wittenberg, D. L. Rousseau & M. Guertin Eur. J. Biochem. 267, 4770-4780 (2000). 180. Hierarchical Folding of Cytochrome c. S.-R. Yeh & D. L. Rousseau Nature Struct. Biol. 7, 443-445 (2000). 179. Distal Interactions in the Cyanide Complex of Ferric Chlamydomonas Hemoglobin. T. K. Das, M. Couture, M. Guertin & D. L. Rousseau J. Phys. Chem. B, 104, 10750-10756 (2000). 178. pH-Dependent Structural Changes at the Heme-Copper Binuclear Center of Cytochrome c Oxidase. T. K. Das, F. L. Tomson, R. B. Gennis, M. Gordon & D. L. Rousseau Biophys. J. 80, 2039-2045 (2001). 177. Origin of the Anomalous Fe-CO Stretching Mode in the CO Complex of Ascaris Hemoglobin. T. K. Das, J. M. Friedman, A. P. Kloek, D. E. Goldberg & D. L. Rousseau Biochemistry 39, 837-842 (2000). 176. The Ferrous Dioxygen Complex of the Oxygenase Domain of Neuronal Nitric Oxide Synthase. M. Couture, D. J. Stuehr & D. L. Rousseau J. Biol. Chem. 275, 3201-3205 (2000). 175. Mutations in the Putative H-channel in the Cytochrome Oxidase from Rhodobacter sphaeroides show that this Channel is not Important for Proton Conduction but reveal Modulation of the Properties of Heme a. H.-m. Lee, T. K. Das, D. L. Rousseau, D. Mills, S. Ferguson-Miller & R. B. Gennis Biochemistry 39, 2989-2996 (2000). 174. A Cooperative oxygen Binding Hemoglobin from Mycobacterium tuberculosis: Stabilization of Heme Ligands by a Distal Tyrosine Residue. S.-R. Yeh, M. Couture, Y. Ouellet, M. Guertin & D. L. Rousseau J. Biol. Chem. 275, 1679-1684 (2000). 173. Pentacoordinate Hemin Derivatives in Sodium Dodecyl Sulfate Micelles: Model Systems for the Assignment of the Fifth Ligand in Ferric Heme Proteins. A. Boffi, T. K. Das, S. della Longa, C. Spagnuolo & D. L. Rousseau Biophys. J. 77, 1143-1149 (1999). 172. Stopped-Flow Analysis of Substrate Binding to Neuronal Nitric Oxide Synthase. H. M. Abu-Soud, J. Wang, D. L. Rousseau & D. J. Stuehr Biochemistry 38, 12446-12451 (1999). 171. Time-Dependence of the Catalytic Intermediates in Cytochrome c Oxidase. S. Han, S. Takahashi & D. L. Rousseau J. Biol. Chem. 275, 1910-1919 (2000). 170. Bioenergetics: Two Phases of Proton Translocation. D. L. Rousseau Nature 400, 412-413 (1999). 169. Temperature Dependent Quaternary State Relaxation in Sol-Gel Encapsulated Hemoglobin. T. K. Das, I. Khan, D. L. Rousseau & J. M. Friedman Biospectroscopy 5, S64-S70 (1999). 168. Submillisecond Unfolding Kinetics of Apomyoglobin and its pH 4 Intermediate. M. Jamin, S.-R. Yeh, D. L. Rousseau & R. L. Baldwin J. Mol. Biol. 292, 731-740 (1999). 167. Identification of the Ligands to Ferric Heme of Chlamydomonas Chloropast Hemoglobin: Evidence for Ligation of Tyrosine-63 (B10) to the Heme. M. Couture, T. K. Das, H. C. Lee, J. Peisach, D. L. Rousseau, B. A. Wittenberg & J. B. Wittenberg Biochemistry 38, 15360-15368 (1999). 166. A Cooperative Oxygen Binding Hemoglobin from Mycobacterium tuberculosis. M. Couture, S.- R. Yeh, B. A. Wittenberg, J. B. Wittenberg, Yannick Ouellet, D. L. Rousseau & M. Guertin Proc. Nat. Acad. Sci. USA 96, 11223-11228 (1999). 165. Redox-Linked Transient Deprotonation at the Binuclear Site in the aa3-type Quinol Oxidase from Acidianus ambivalens: Implications for proton translocation. T. K. Das, C. M. Gomes, M. Teixeira & D. L. Rousseau Proc. Nat. Acad. Sci. USA 96, 9591-9596 (1999). 164. Ligand Exchange During Unfolding of Cytochrome c. S.-R. Yeh & D. L. Rousseau J. Biol. Chem. 274, 17853-17859 (1999). 163. Formation of a Five-Coordinate Hydroxide-Bound Heme in the His93Gly Mutant of Sperm Whale Myoglobin. T. K. Das, S. Franzen, A. Pond, J. H. Dawson & D. L. Rousseau Inorganic Chem. 38, 1952-1953 (1999). 162. Chlamydomonas Chloroplast Ferrous Hemoglobin: Heme Pocket Structure and Reactions with Ligands. M. Couture, T. K. Das, H. C. Lee, J. Peisach, D. L. Rousseau, B. A. Wittenberg & J. B. Wittenberg J. Biol. Chem. 274, 6898-6910 (1999). 161. Hydroxide rather than Histidine is Coordinated to the Heme in Five-Coordinate Ferric Scapharca inaequivalvis Hemoglobin. T. K. Das, A. Boffi, E. Chiancone & D. L. Rousseau J. Biol. Chem., 274, 2916-2919 (1999). 160. The Heme Environment in Barley Hemoglobin. T. K. Das, H. C. Lee, S. M. G. Duff, R. D. Hill, J. Peisach, D. L. Rousseau, B. A. Wittenberg & J. B. Wittenberg J. Biol. Chem., 274, 4207-4212 (1999). 159. The Post-Translational Modification in Cytochrome c Oxidase is Required to Establish a Functional Environment of the Catalytic Site. T. K. Das, C. Pecoraro, F. L. Tomson, R. B. Gennis & D. L. Rousseau Biochemistry 37, 14471-14476 (1998). 158. The Apolar Distal Histidine Mutant (His69Val) of the Homodimeric Scapharca Hemoglobin is in an R-like Conformation. L. Guarrera, G. Colotti, A. Boffi, E. Chiancone, T. K. Das, D. L. Rousseau & Q. Gibson Biochemistry 37, 5608-5615 (1998). 157. Domain Swapping in Inducible NO Synthase: Electron Transfer Occurs Between Flavin and Heme Groups Located on Adjacent Subunits in the Dimer. U. Siddhanta, A. Presta, B. Fan, D. Wolan, D. L. Rousseau & D. J. Stuehr J. Biol. Chem., 273, 18950-18958 (1998). 156. Cytochrome c Folding and Unfolding: A Biphasic Mechanism. S.-R. Yeh, S. Han & D. L. Rousseau Acc. Chem. Res., 31, 727-736 (1998). 155. Preservation of the Native Structure in Myoglobin at Low pH by Sol-Gel Encapsulation. T. K. Das, I. Khan, D. L. Rousseau & J. M. Friedman J. Am. Chem. Soc. 120, 10268-10269 (1998). 154. Folding Intermediates in Cytochrome c. S.-R. Yeh & D. L. Rousseau Nature Struct. Biol., 5, 222-228 (1998). 153. Resonance Raman Characterization of Soluble Guanylyl Cyclase Expressed from Baculovirus. B. Fan, G. Gupta, R. S. Danziger, J. Friedman & D. L. Rousseau Biochemistry, 37, 1178-1184 (1998). 152. NO Synthase Isozymes have Distinct Substrate Binding Sites. B. Fan, J. Wang, D. J. Stuehr & D. L. Rousseau Biochemistry 36, 12660-12665 (1997). 151. Heme Oxygenase. A Central Enzyme of Oxygen-Dependent Heme Catabolism and Carbon Monoxide Synthesis. M. Ikeda-Saito, H. Fujii, K. Mansfield-Matera, S. Takahashi, C. T. Migita, D. L. Rousseau & T. Yoshida Oxygen Hemeostasis and Its Dynamics; Edited by Y. Ishimura (Springer-Verlag) 1997, in press. 150. Sequence Specific Changes in the Metal Site of Ferric Bleomycin Induced by the Binding of DNA. J. W. Sam, S. Takahashi, J. Peisach & D. L. Rousseau J. Biol. Chem., 26, 16090-16097 (1998). 149. Dynamics of Cyanide Binding to Ferrous Scapharca Inaequivalvis Homodimeric Hemoglobin. A. Boffi, E. Chiancone, E. Peterson, J. Wang, D. L. Rousseau & J. M. Friedman Biochemistry 36, 4510-4514 (1997). 148. Steriochemistry of the FeII- and FeIII- Cyanide Complexes of the Homodimeric Scapharca Inaequivalvis Hemoglobin. A Resonance Raman and FTIR Study. A. Boffi, E. Chiancone, S. Takahashi & D. L. Rousseau Biochemistry 36, 4505-4509 (1997). 147. The Unique Heme-Heme Interactions of the Homodimeric Scapharca Inaeqivalvis Hemoglobin as Probed in the Protein Reconstituted with unnatural 2,4 Heme Derivatives. C. Zamparelli, D. Verzili, A. Boffi, E. Chiancone, S. Takahashi, D. L. Rousseau, R. Regan & Q. Gibson Arch. Biochem. Biophys. 339, 275-282 (1997). 146. Interactions Between Substrate Analogues and Heme Ligands in NO Synthase. J. Wang, D. J. Stuehr & D. L. Rousseau Biochemistry 36, 4595-4606 (1997). 145. Resonance Raman Characterization of -Hydroxyheme and Verdoheme Complexes of Heme Oxygenase. S. Takahashi, K. Mansfield Matera, H. Fujii, H. Zhou, K. Ishikawa, T. Yoshida, M. Ikeda-Saito & D. L. Rousseau Biochemistry 36, 1402-1410 (1997). 144. Submillisecond Protein Folding Kinetics Studied by Ultrarapid Mixing. C.-K. Chan, Y. Hu, S. Takahashi, D. L. Rousseau, W. A. Eaton & J. Hofrichter Proc. Nat. Acad. Science (USA) 94, 1779-1784 (1997). 143. Ligand Exchange During Cytochrome c Folding. S.-R. Yeh, S. Takahashi, B. Fan & D. L. Rousseau Nature Struct. Biol. 4, 51-56 (1997). 142. Folding of Cytochrome c Initiated by Submillisecond Mixing. S. Takahashi, S.-R. Yeh, T. K. Das, C.-K. Chan, D. S. Gottfried & D. L. Rousseau Nature Struct. Biol. 4, 44-50 (1997). 141. Nitric Oxide Binding to the Heme of Neuronal Nitric Oxide Synthase Links Its Activity to Changes in Oxygen Tension. H. M. Abu-Soud, D. L. Rousseau & D. J. Stuehr J. Biol. Chem. 271, 32515-32518 (1996). 140. Electric-Field-Induced Schiff-Base Deprotonation in D85N Mutant Bacteriorhodopsin. P. Kolodner, E. P. Lukashev, Y.-c. Ching & D. L. Rousseau Proc. Nat. Acad. Sci. (USA) 93, 11618-11621 (1996). 139. Oxygen and One Reducing Equivalent are Both Required for the Conversion of a-Hydroxyhemin to Verdoheme in Heme Oxygenase. K. Mansfield Matera, S. Takahashi, H. Fujii, Z. Hong, K. Ishikawa, T. Yoshimura, D. L. Rousseau, T. Yoshida, & M. Ikeda-Saito J. Biol. Chem. 271, 6618-6624 (1996). 138. The Crystal Structure of Cytochrome c Oxidase. D. L. Rousseau Physics News in 1995, 19-20 (1996). 137. Control of Electron Transfer in Neuronal NO Synthase by Calmodulin, Substrate, Substrate Analogs and NO. D. J. Stuehr, H. M. Abu-Soud, D. L. Rousseau, P. L. Feldman & J. Wang Nitric Oxide: Biochemistry, Molecular Biology and Therapeutic Implications; Eds. L. Ignarro & F. Murad; Vol 34 of Advances in Pharmacology, pp. 207-213 (1995). 136. Cytochrome c Peroxidase Complexed with Cytochrome c has an Unperturbed Heme Moiety. J. Wang, R. W. Larson, S. J. Moench, J. D. Satterlee, D. L. Rousseau & M. R. Ondrias Biochemistry 35, 453-463 (1996). 135. The Reaction of Cytochrome bo3 with Oxygen: Extra Redox Center(s) are Present in the Protein. J. Wang, J. Rumbley, Y.-c. Ching, S. Takahashi, R. B. Gennis & D. L. Rousseau Biochemistry 34, 15504-15511 (1995). 134. Neuronal NO Synthase Self-Inactivates by Forming a Ferrous-Nitrosyl Complex During Aerobic Catalysis. H. M. Abu-Soud, J. Wang, D. L. Rousseau, J. M. Fukuto, L. J. Ignarro & D. J. Stuehr J. Biol. Chem. 270, 22997-23006 (1995). 133. The cbb3-Type Cytochrome c Oxidase from Rhodobacter capsulatus Contains a Unique Active Site. J. Wang, K. A. Gray, F. Daldal & D. L. Rousseau J. Am. Chem. Soc.,117, 9363-9364 (1995). 132. Two Conformations of the Catalytic Site in the aa3-Type Cytochrome c oxidase from Rhodobacter sphaeroides. J. Wang, S. Takahashi, J. P. Hostler, S. Ferguson-Miller, D. M. Mitchell, R. B. Gennis & D. L. Rousseau Biochemistry, 34, 9819-9825 (1995). 131. Methods for Analysis and Detection of Nitric Oxide by Infrared Spectroscopy. V. Sampath, D. L. Rousseau & W. S. Caughey Methods in Nitric Oxide Research; Edited by M. Feelisch & J. Stamler (Wiley) 1996, pp. 413-426. 130. Resonance Raman Scattering: A Probe of NO-Bound Hemeproteins. J. Wang, W. S. Caughey & D. L. Rousseau Methods in Nitric Oxide Research; Edited by M. Feelisch & J. Stamler (Wiley) 1996, pp. 427-454. 129. Heme Oxygenase-2: Properties of the Heme Complex and Purified Tryptic Fragment of Recombinant Human Heme Oxygenase-2. K. Ishikawa, N. Takeuchi, S. Takahashi, K. Mansfield -Matera, M. Sato, S. Shibahara, D. L. Rousseau, M. Ikeda-Saito & T. Yoshida J. Biol. Chem., 270, 6345-6350 (1995). 128. Microsecond Generation of Oxygen-Bound Cytochrome c Oxidase by Rapid Solution Mixing. S. Takahashi, Y.-c. Ching, J. Wang & D. L. Rousseau J. Biol. Chem., 270, 8405-8407 (1995). 127. Tetrahydrobiopterin-Deficient Nitric Oxide Synthase Has a Modified Heme and Forms a Cytochrome P-420 Analogue. J. Wang, D. J. Stuehr & D. L. Rousseau Biochemistry, 34, 7080-7087 (1995). 126. Identification of the Overtone of the Fe-CO Stretching Mode in Hemoproteins: A New Active Site Probe. J. Wang, S. Takahashi & D. L. Rousseau Proc. Nat. Acad. Sci. (USA), 92, 9402-9406 (1995). 125. A Synthetic Analogue for the Oxygen Binding Site in Cytochrome c Oxidase. J. P. Collman, P. C. Herrmann, B. Boitrel, X. Zhang, T. A. Eberspacher, L. Fu, J. Wang, D. L. Rousseau & E. R. Williams J. Am. Chem. Soc. 116, 9783-9784 (1994). 124. Oxygen-Bound Heme-Heme Oxygenase Complex: Evidence for a Strongly Bent Structure of the Coordinated Oxygen. S. Takahashi, D. L. Rousseau, K. Ishikawa, T. Yoshida & M. Ikeda-Saito J. Am. Chem. Soc., 117, 6002-6006 (1995). 123. Heme Coordination of NO in Nitric Oxide Synthase. J. Wang, D. L. Rousseau, H. M. Abu-Soud & D. J. Stuehr Proc. Nat. Acad. Sci. (USA), 91, 10512-10516 (1994). 122. Coordination and Spin State Equilibria as a Function of pH, Ionic Strength, and Protein Concentration in Oxidized Dimeric Scapharca Inaequivalvis Hemoglobin. C. Spagnuolo, F. DeMartino, A. Boffi, D.L. Rousseau & Emilia Chiancone J. Biol. Chem. 269, 20441-20445 (1994). 121. Structural Characterization of Oxidized Dimeric Scapharca Inaequivalvis Hemoglobin by Resonance Raman Spectroscopy. A. Boffi, S. Takahashi, C. Spagnuolo, D. L. Rousseau & E. Chiancone J. Biol. Chem. 269, 20437-20440 (1994). 120. Heme-Heme Oxygenase Complex: Structural and Properties of the Catalytic Site from Resonance Raman Scattering. S. Takahashi, J. Wang, D. L. Rousseau, K. Ishikawa, T. Yoshida, N. Takeushi & M. Ikeda-Saito Biochemistry 33, 5531-5538 (1994). 119. Structural Characterization of Iron-Bleomycin by Resonance Raman Spectroscopy. S. Takahashi, J. W. Sam, J. Peisach & D. L. Rousseau J. Am. Chem. Soc. 116, 4408-4413 (1994). 118. Heme-Heme Oxygenase Complex:Structure of the Catalytic Site and its Implications for Oxygen Activation. S. Takahoshi, J. Wang, D. L. Rousseau, K. Ishikawa, T. Koshida, J. R. Host & M. Ikeda-Saito J. Biol. Chem. 269, 1010-1014 (1994). 117. Metastable Structures of the Carbon Monoxide Photoproduct in a Novel Dimeric Hemoglobin. S. Song, L. Rothberg, D. L. Rousseau, A. Boffi & E. Chiancone Biophysical J. 65, 1959-1962 (1993). 116. Heme Coordination and Structure of the Catalytic Site in Nitric Oxide Synthase. J. Wang, D. J. Stuehr, M. Ikeda-Saito & D. L. Rousseau J. Biol. Chem. 268, 22255-22258 (1993). 115. Protein-Heme Interactions in Hemoglobin from the Mollusc Scapharca Inaequivalvis: Evidence from Resonance Raman Scattering. S. Song, A. Boffi, E. Chiancone & D. L. Rousseau Biochemistry 32, 6330-6336 (1993). 114. Similar CO Binding Sites in Bacterial Cytochrome bo and Mammalian Cytochrome c Oxidase. J. Wang, Y.-c. Ching, D. L. Rousseau, J. J. Hill, J. Rumbley & R. B. Gennis J. Am. Chem. Soc. 115, 3390-3391 (1993). 113. Heme-Heme Interaction in a Homodimeric Cooperative Hemoglobin: Evidence from Transient Raman Scattering. D. L. Rousseau, S. Song, J. M. Friedman, A. Boffi & E. Chiancone J. Biol. Chem. 268, 5719-5723 (1993). 112. Proton Translocation in Cytochrome c Oxidase: Redox Linkage Through Proximal Ligand Exchange on Cytochrome a3. D. L. Rousseau, Y.-c. Ching & J. Wang J. of Bioenerg. Biomemb. 25, 165-176 (1993). 111. The Catalytic Mechanism of Cytochrome c Oxidase. D. L. Rousseau, S. Han, S. Song & Y.-c. Ching J. Raman Spectrosc. 23, 551-556 (1992). 110. Hydrogen Bonding of Iron-Coordinated Histidine in Heme Proteins. D. G. Rousseau & D. L. Rousseau J. Structural Biol. 109, 13-17 (1992). 109. Case Studies in Pathological Science. D. L. Rousseau American Scientist 80, 54-63 (1992). 108. Intermediates Formed in the Reaction of Cytochrome c Oxidase with Oxygen. S. Han, S. Song, Y.-c. Ching & D. L. Rousseau Time Resolved Vibrational Spectroscopy; Edited by H. Takahashi (Springer-Verlag) 1992 pp. 20-23. 107. Vibrational Structure of the Formyl Group on Heme a: Implications on the Properties of Cytochrome c Oxidase. S. Han, Y.-c Ching, S. L. Hammes & D. L. Rousseau Biophysical J. 60, 45-62 (1991). 106. Biophysics. D. L. Rousseau and L. W. Jelinski Encyclopedia of Applied Physics, Vol. 2, 1991, pp. 571-608. 105. Ferryl and Hydroxy Intermediates in the Reaction of Oxygen with Reduced Cytochrome c Oxidase. S. Han, Y.-c. Ching & D. L. Rousseau Nature 348, 89-90 (1990). 104. Cytochrome c Oxidase: Decay of the Primary Intermediate Involves Direct Electron Transfer from Cytochrome a. S. Han, Y.-c. Ching & D. L. Rousseau Proc. Nat. Acad. Sci. (USA) 87, 8408-8412 (1990). 103. Time Evolution of Intermediates Formed in the Reaction of Oxygen with Mixed Valence Cytochrome c Oxidase. S. Han, Y.-c. Ching & D. L. Rousseau J. Am. Chem. Soc. 112, 9445-9451 (1990). 102. Primary Intermediate in the Reaction of Oxygen with Fully Reduced Cytochrome c Oxidase. S. Han, Y.-c. Ching & D. L. Rousseau Proc. Nat. Acad. Sci. (USA) 87, 2491-2495 (1990). 101. Primary Intermediate in the Reaction of Mixed Valence Cytochrome c Oxidase with Oxygen. S. Han, Y.-c. Ching & D. L. Rousseau Biochemistry 29, 1380-1384 (1990). 100. Metastable Intermediates in Myoglobin at Low pH. S. Han, D. L. Rousseau, G. Giacometti & M. Brunori Proc. Nat. Acad. Sci. (USA) 87, 205-209 (1990). 99. Cytochrome c Oxidase: The Influence of the "Open-Closed" Transition on Cytochrome a3 D. L. Rousseau, Y.-c. Ching & S. Han SPIE 1055, 244-253 (1989). 98. Evidence for a Hydroxide Intermediate in Cytochrome c Oxidase. S. Han, Y.-c. Ching & D. L. Rousseau J. Biol. Chem. 264, 6604-6607 (1989). 97. Spin Equilibrium in Human Methemoglobin: The Effects of Inositol Hexaphosphate and Bezafibrate as Measured by Resonance Raman Spectroscopy. R. W. Noble, A. DeYoung & D. L. Rousseau Biochemistry 28, 5293-5297 (1989). 96. Axial Coordination of Ferric Aplysia Myoglobin. D. L. Rousseau, Y.-c. Ching, M. Brunori & G. M. Giacometti J. Biol. Chem. 264, 7878-7881 (1989). 95. The Role of Water Near Cytochrome a in Cytochrome c Oxidase. D. L. Rousseau, M. Sassaroli, Y.-c. Ching & S. Dasgupta Annals N.Y. Acad. Sci. 550, 223-237 (1988). 94. Cytochrome c Oxidase: Evidence for Interaction of Water Molecules with Cytochrome a. M. Sassaroli, Y.-c. Ching, S. Dasgupta & D. L. Rousseau Biochemistry 28, 3128-3132 (1989). 93. Structural Characterization of Cytochrome c Peroxidase by Resonance Raman Scattering. S. Dasgupta, D. L. Rousseau, H. Anni &T. Yonetani J. Biol. Chem. 264, 654-662 (1989). 92. Nitrosyl Cytochrome c Oxidase: Formation and Properties of the Mixed-Valence Enzyme. D. L. Rousseau, S. Singh, Y.-c. Ching & M. Sassaroli J. Biol. Chem. 263, 5681-5685 (1988). 91. Photodissociated Cytochrome c Oxidase: Cryotrapped Metastable Intermediates. M. Sassaroli, Y.-c. Ching, P. V. Argade & D. L. Rousseau Biochemistry 27, 2496-2502 (1988). 90. Transient and Cryogenic Studies of Photodissociated Hemoglobin and Myoglobin. D. L. Rousseau & J. M. Friedman Biological Applications of Raman Spectroscopy, Vol. 3; Edited by T. G. Spiro (Wiley) 1988, pp. 134-215. 89. Time Dependence of Near Infrared Spectra of Photodissociated Hemoglobin and Myoglobin. M. Sassaroli & D. L. Rousseau Biochemistry 26, 3092-3098 (1987). 88. Simulation of Carboxymyoglobin Photodissociation. M. Sassaroli & D. L. Rousseau J. Biol. Chem. 261, 16292-16294 (1986). 87. Structure and Dynamics of Photodissociated Myoglobin. D. L. Rousseau, M. Sassaroli & S. Dasgupta Structure, Dynamics, and Function of Biomolecules; Edited by A. Ehrenberg and R. Rigler (Springer- Verlag) 1987 pp. 25-29. 86. Cryogenic Stablization of Myoglobin Photoproducts. M. Sassaroli, S. Dasgupta & D. L. Rousseau J. Biol. Chem. 261, 13704-13713 (1986). 85. Accessibility of the Cytochrome a Heme in Cytochrome c Oxidase to Exchangeable Protons. P. V. Argade, Y.-c. Ching, M. Sassaroli & D. L. Rousseau J. Biol. Chem. 261, 5969-5973 (1986). 84. Metastable Photoproducts from Carbon Monoxy Myoglobin. D. L. Rousseau & P. V. Argade Proc. Nat. Acad. Sci. (USA) 83, 1310-1314 (1986). 83. Resonance Raman Isolation of the a and a3 Chromophores in Cytochrome Oxidase. P. V. Argade, Y.-c. Ching & D. L. Rousseau Biophysical J. 50, 613-620 (1986). 82. Book Review: "Applications of Infrared, Raman, and Resonance Raman Spectroscopy in Biochemistry" by F. S. Parker. D. L. Rousseau The Quarterly Review of Biology 60, 70-71 (1985). 81. Probing Molecular Motions in Heme Proteins. D. L. Rousseau Physics Today 38, S-14 (1985). 80. Resonance Raman Spectra of CN--Bound Cytochrome Oxidase: Spectral Isolation of Cytochromes a2+, a32+, and a32+ (CN-). Y.-c. Ching, P. V. Argade & D. L. Rousseau Biochemistry 24, 4938-4946 (1985). 79. Resonance Raman Evidence of Chloride Binding to the Heme Iron in Myeloperoxidase. M. Ikeda-Saito, P. V. Argade & D. L. Rousseau FEBS Letters 184, 52-55 (1985). 78. Spectroscopic Studies of Protein-Heme Interactions Accompanying the Allosteric Transition in Methemoglobins. E. R. Henry, D. L. Rousseau, J. J. Hopfield, R. W. Noble & S. R. Simon Biochemistry 24, 5907-5918 (1985). 77. Resonance Raman Spectra of Photodissociated Hemoglobins: Implications on Cooperative Mechanisms. D. L. Rousseau & M. R. Ondrias Biophysical J. 47, 537-545 (1985). 76. Confirmation of the Assignment of the Iron-Histidine Stretching Mode in Myoglobin. P. V. Argade, M. Sassaroli, D. L. Rousseau, T. Inubushi, M. Ikeda-Saito & A. Lapidot J. Am. Chem. Soc. 106, 6593-6596 (1984). 75. Cytochrome a3 Structure in Carbon Monoxide-Bound Cytochrome Oxidase. P. V. Argade, Y.-c. Ching & D. L. Rousseau Science 255, 329-331 (1984). 74. Raman Scattering. D. L. Rousseau and M. R. Ondrias Physical Techniques in Biology and Medicine.;Vol. I: Optical Techniques in Biological Research. Edited by D. L. Rousseau (Academic Press) 1984, pp. 65-132. 73. Absence of Cooperative Energy at the Heme in Liganded Hemoglobins. D. L. Rousseau, S. L. Tan, M. R. Ondrias, S. Ogawa & R. W. Noble Biochemistry 23, 2857-2865 (1984). 72. Resonance Raman Spectra of Photodissociated Carbon Monoxy Hemoglobin (Hb*) at Cryogenic Temperatures. D. L. Rousseau, M. R. Ondrias & J. M. Friedman Time-Resolved Vibrational Spectroscopy, ed. by G. H. Atkinson (Academic Press) 1983, pp 317-324. 71. Resonance Raman Spectra of the Heme in Leghemoglobin: Evidence for the Absence of Ruffling and the Influence of the Vinyl Groups. D. L. Rousseau, M. R. Ondrias, G. N. LaMar & K. M. Smith J. Biol. Chem. 258, 1740-1746 (1983). 70. Metastable Species of Hemoglobin: A Comparison of Room Temperature Transients and Cryogenically Trapped Intermediates. M. R. Ondrias, J. M. Friedman & D. L. Rousseau. Science 220, 615-617 (1983). 69. Resonance Raman Scattering Studies of the Quaternary Structure Transition in Hemoglobin. D. L. Rousseau & M. R. Ondrias Ann. Rev. Biophys. Bioeng. 12, 357-389 (1983). 68. Resonance Raman Spectra of Photodissociated Carbonmonoxy Hemoglobin (Hb*) and Deoxy Hemoglobin at 10°K. M. R. Ondrias, D. L. Rousseau & S. R. Simon J. Biol. Chem. 258, 5638-5642 (1983). 67. Time Resolved Resonance Raman Studies of Hemoglobins. J. M. Friedman, D. L. Rousseau & M. R. Ondrias Ann. Rev. Phys. Chem. 33, 471-491 (1982). 66. Quaternary Transformation Induced Changes at The Heme in Deoxyhemoglobins. M. R. Ondrias, D. L. Rousseau, J. A. Shelnutt & S. R. Simon Biochemistry 21, 3428-3437 (1982). 65. Resonance Raman Evidence for Hydrogen Bonding of Bound Dioxygen to the Distal Histidine of Oxy Cobalt Myoglobin and Hemoglobin. T. Kitagawa, M. R. Ondrias, D. L. Rousseau, M. Ikeda-Saito & T. Yonetani Nature 298, 869-871 (1982). 64. Quaternary Structure Changes in Iron-Cobalt Hybrid Hemoglobins Detected by Resonance Raman Scattering. M. R. Ondrias, D. L. Rousseau, T. Kitagawa, M. Ikeda-Saito, T. Inubushi & T. Yonetani J. Biol. Chem. 257, 8766-8770 (1982). 63. Transient Raman Study of Hemoglobin: Structural Dependence of the Iron-Histidine Linkage. J. M. Friedman, D. L. Rousseau, M. R. Ondrias & R. A. Stepnoski Science 218, 1244-1246 (1982). 62. Resonance Raman Spectra of Heme c and Heme d1 in Pseudomonas Cytochrome Oxidase. Y.-c. Ching, M. R. Ondrias, D. L. Rousseau, B. B. Mahoberac & D. C. Wharton FEBS Letters 138, 239-244 (1982). 61. Resonance Raman Detection of Structural Dynamics at the Active Site in Hemoglobin. M. R. Ondrias, D. L. Rousseau & S. R. Simon Proc. Nat. Acad. Sci. (USA) 79, 1511-1514 (1982). 60. Structural Changes at the Heme Induced by Freezing Hemoglobin. M. R. Ondrias, D. L. Rousseau & S. R. Simon Science 213, 657-659 (1981). 59. Protein Influences on Porphyrin Structure in Cytochrome c: Evidence from Raman Difference Spectroscopy. J. A. Shelnutt, D. L. Rousseau, J. K. Dethmers & E. Margoliash Biochemistry 20, 6485-6497 (1981). 58. Normal Mode Determination in Crystals. D. L. Rousseau, R. P. Bauman & S. P. S. Porto J. Raman. Spectrosc. 10, 253-290 (1981). 57. Raman Difference Spectroscopy as a Probe of Biological Molecules. D. L. Rousseau J. Raman Spectrosc. 10, 94-99 (1981). 56. Charge Transfer Stabilization of Hemoglobin Structures. D. L. Rousseau, J. A. Shelnutt, J. M. Friedman, E. R. Henry & S. R. Simon Biophys. J. 32, 83-85 (1980). 55. An Electronic Interaction Model for Hemoglobin Cooperativity: Evidence From Raman Difference Spectroscopy. D. L. Rousseau, J. A. Shelnutt, M. R. Ondrias, J. M. Friedman, E. R. Henry & S. R. Simon Hemoglobin and Oxygen Binding;ed. by C. Ho (Elsevier North Holland, Inc.) 1982 pp. 224-229. 54. Raman Difference Spectroscopy of Tertiary and Quaternary Structure Changes in Methemoglobins. D. L. Rousseau, J. A. Shelnutt, E. R. Henry & S. R. Simon Nature 285, 49-51 (1980). 53. Methemoglobin Imidazole: Evidence Against an IHP-Induced Change in Quaternary Structure. D. L. Rousseau, J. A. Shelnutt & S. R. Simon FEBS Letters 111, 235-239 (1980). 52. Br2 in an Ar Matrix: An Example of Complete Damping of the Resonance Raman Scattering Amplitude in the Discrete Resonance Limit. J. M. Friedman, V. E. Bondybey & D. L. Rousseau Chem. Phys. Letters 70, 499-503 (1980). 51. Protein-Heme Interaction in Hemoglobin: Evidence From Raman Difference Spectroscopy. J. A. Shelnutt, D. L. Rousseau, J. M. Friedman & S. R. Simon Proc. Nat. Acad. Sci.(USA) 76, 4409-4413 (1979). 50. Protein Influence on the Heme in Cytochrome c: Evidence From Raman Difference Spectroscopy. J. A. Shelnutt, D. L. Rousseau, J. K. Dethmers & E. Margoliash Proc. Nat. Acad. Sci. (USA) 76, 3865-3869 (1979). 49. The Effect of Deuteration on the Carboxyl Stretching Frequencies of a Salicylic Adic Derivative. J. M. Friedman, D. L. Rousseau & C. Shen Spectrochim Acta 35A, 989-991 (1979). 48. Ruthenium Red as a Resonance Raman Probe of Ca2+ Binding Sites in Biological Materials. J. M. Friedman, D. L. Rousseau, G. Navon, S. Rosenfeld, P. Glynn & K. B. Lyons Arch. Biochem. Biophys. 192, 14-21 (1979). 47. Lasalocid Crystallized From Methanol: Spectroscopic and X-ray Structural Evidence for Two Structures. J. M. Friedman, D. L. Rousseau, C. Shen, C. L. Chiang, E. N. Duessler & I. C. Paul J.C.S. Perkins Trans. II 1979, 835-838. 46. The Resonance Raman Effect. D. L. Rousseau, J. M. Friedman & P. F. Williams Topics in Current Physics Vol. II: Raman Spectroscopy of Gases and Liquids ed. by A. Weber, (Springer-Verlag) 1979, pp. 203-252. 45. Liquid and Solid Phase Regrowth of Si by Laser Irradiation and Thermally Assisted Flash Annealing. J. M. Poate, J. C. Bean, W. L. Brown, R. L. Cohen, L. C. Feldman, H. J. Leamy, J. W. Rodgers, D. L.Rousseau, G. A. Rozgonyi, J. A. Shelnutt, T. T.Sheng, K. W. West, J. S. Williams & G. K. Celler Radiation Effects 48, 167-173 (1980). 44. Solid-Phase Epitaxy of Implanted Silicon by CW Ar Ion Laser Irradiation. J. S. Williams, W. L. Brown, H. J. Leamy, J. M. Poate, J. W. Rodgers, D. L. Rousseau, G. A. Rozgonyi, J. A. Shelnutt & T. T. Sheng Appl. Phys. Letters 33, 542-544 (1978). 43. Simultaneous Observation of Coherent and Incoherent Resonant Re-emission in the Condensed Phase. J. M. Friedman & D. L. Rousseau Chem. Phys. Letters 55, 488-492 (1978). 42. Infrared Evidence For Hydrogen Bonding in the Sodium Salts of Lasalocid (X-537A). J. M. Friedman, D. L. Rousseau, C. Shen & I. C. Paul J.C.S. Chem. Comm. 1977, 684-686. 41. Excited State Lifetimes in Cytochromes Measured From Raman Scattering Data: Evidence for Iron- Porphyrin Interactions. J. M. Friedman, D. L. Rousseau & F. Adar Proc. Nat. Acad. Sci. (USA) 74, 2607-2611 (1977). 40. Evidence for Excited Electronic State Interference in Resonance Raman Scattering. P. Baierl, W. Kieffer, P. F. Williams, and D. L.Rousseau Chem. Phys. Letters 50, 57-60 (1977). 39. Experimental Measurement of Dissociative Molecular Potential Functions From Continuum Resonance Raman Spectra. P. F. Williams, A. Fernandez & D. L. Rousseau Chem. Phys. Letters 47, 150-154 (1977). 38. Origin of Resonant Raman Excitation Profiles Red-Shifted From Optical Absorption Profiles. J. M. Friedman, D. L. Rousseau & V. E. Bondybey Phys. Rev. Letters 37, 1610-1613 (1976). 37. Reply to "Comment on 'Resonance Raman Scattering and Collision-Induced Redistribution Scattering in I2'".D. L. Rousseau, G. D. Patterson & P. F. Williams Phys. Rev. Letters 37, 1441-1444 (1976). 36. Resonance Raman Scattering of Light From a Diatomic Molecule.D. L. Rousseau & P. F. Williams Proceedings of the 5th International Conference on Raman Spectroscopy 1976 pp. 257-266. 35. Comment on "Two-Magnon Resonant Raman Scattering in MnF2". D. L. Rousseau, R. E. Dietz, P. F. Williams & H. J. Guggenheim. Phys. Rev. Letters 36, 1098-1101 (1976). 34. Resonance Raman Scattering of Light From a Diatomic Molecule. D. L. Rousseau & P. F. Williams J. Chem. Phys. 64, 3519-3537 (1976). 33. Lifetime of E>B Transition in Molecular Iodine. D. L. Rousseau J. Mole. Spect. 58, 481-483 (1975). 32. Resonance Raman Scattering and Collision-Induced Redistribution Scattering in I2. D. L. Rousseau, G. D. Patterson & P. F. Williams Phys. Rev. Letters 34, 1306-1309 (1975). 31. Discrete and Diffuse Emission Following Two-Photon Excitation of the E State in Molecular Iodine. D. L. Rousseau & P. F. Williams Phys. Rev. Letters 33, 1368-1372 (1974). 30. Dependence of the Electronic Transition Moment on Internuclear Separation in Na2: A Quantum Mechanical Treatment. P. F. Williams and D. L. Rousseau Phys. Rev. Letters 33, 1516-1520 (1974). 29. Raman Scattering and Infrared Absorption from the C-N Stretching Modes of K2Pt(CN)4 Br0.3•3 H2O. D. L. Rousseau, M. A. Butler, H. J. Guggenheim, R. B. Weisman & A. N. Bloch Phys. Rev. B10, 2281-2285 (1974). 28. Optical Excitation of Plasmons in a Quasi-One-Dimensional Conductor. P. F. Williams, M. A. Butler, D. L. Rousseau & A. N. Bloch Phys. Rev. B10, 1109-1112 (1974). 27. Resonance Fluorescence and Resonance Raman Scattering: Lifetimes in Molecular Iodine. P. F. Williams, D. L. Rousseau & S. H. Dworetsky Phys. Rev. Letters 32, 196-199 (1974). 26. Iron Oxide-An Inorganic Photoresist and Mask Material. W. R. Sinclair, D. L. Rousseau & J. J. Stancavish J. Electrochem. Soc. 121, 925-928 (1974). 25. Resonance Raman Scattering From Iodine: Spectral Changes with Excitation Frequency. P. F. Williams & D. L. Rousseau. Phys. Rev. Letters 30, 951-954 (1973). 24. Book Review: "Raman Spectra of Molecules and Crystals" by M. M. Sushchinskii. D. L. Rousseau Physics Today 25 (June), 61-62 (1973). 23. Raman Scattering from Magnons and Phonons in FeBO3 and FeF3. A. E. Meixner, R. E. Dietz & D. L. Rousseau Phys. Rev. B7, 3134-3141 (1973). 22. X-Ray Photoelectron Measurements of One-Dimensional Platinum Compounds. M. A. Butler, D. L. Rousseau & D.N.E. Buchanan Phys. Rev. B7, 61-65 (1973). 21. Vibrational Spectroscopy of Liquid Crystals. D. L. Rousseau NSF Conference on "Future Trends in Vibrational Spectroscopy" ed. by G. E. Leroi 1972. 20. Laser Chemistry. D. L. Rousseau "Collected Readings in Inorganic Chemistry Vol. II" edited by G. Galloway 1972, pp. 156-160. 19. "Polywater." D. L. Rousseau McGraw Hill Yearbook of Science and Technology, 1972 pp. 327-330. 18. Thermal Shift of ESCA Binding Energies. M. A. Butler, G. K. Wertheim, D. L. Rousseau & S. Hufner Chem. Phys. Letters 13, 473-476 (1972). 17. Comment on "Required Monochromaticity of an Electron Beam Modulated at Optical Frequencies". L. Pfeiffer, D. L. Rousseau & A. R. Hutson Appl. Phys. Letters 20, 147-148 (1972). 16. A Consideration of the Ruby Laser-Induced Decomposition of Azoethane. D. L. Rousseau, W. E. Falconer & G. E. Leroi Chem. Phys. Letters 13, 45-48 (1972). 15. An Alternative Explanation for Polywater. D. L. Rousseau J. Coll. Interface Sci. 36, 434-442 (1971). 14. Plasma Formation Upon Laser Irradiation of Transparent Dielectric Materials Below the Damage Threshold. B. E. Henderson, R. R. Getty, G. E. Leroi & D. L. Rousseau NBS Special Publication #356 "Damage in Laser Materials: 1971" pp. 31-36. 13. "Polywater" and Sweat: Similarities between the Infrared Spectra. D. L. Rousseau Science 171, 170-172 (1971). 12. "Polywater:" Evidence from Electron Spectroscopy for Chemical Analysis (ESCA) of a Complex Salt Mixture. R. E. Davis, D. L. Rousseau & R. D. Board Science 171, 167-170 (1971). 11. Polywater: Polymer or Artifact? D. L. Rousseau & S. P. S. Porto Science 167, 1715-1719 (1970). 10. Optical Phonons in Sodium Chlorate. C. M. Hartwig, D. L. Rousseau & S.P.S. Porto Phys. Rev. 188, 1328-1335 (1969). 9. Light Scattering Research at the University of Southern California. C. A. Arguello, D. L. Rousseau, R. Luzzi & S. P. S. Porto Materials Res. Bull. 4, 463-475 (1969). 8. First Order Raman Effect in Wurtzite-Type Crystals. C. A. Arguello, D. L. Rousseau, and S. P. S. Porto Phys. Rev. 181, 1351-1363 (1969). 7. Rayleigh Scattering of Linearly Polarized Light from Optically Active Quartz. C. A. Arguello, D. L. Rousseau, S. P. S. Porto, L. E. Cheesman & J. F. Scott Appl. Optics 7, 1913-1915 (1968). 6. Charged-Particle Emission upon Ruby Laser Irradiation of Transparent Dielectric Materials. D. L. Rousseau, G. E. Leroi & W. E. Falconer J. Appl. Phys. 39, 3328-3332 (1968). 5. Auger-Like Resonant Interference in Raman Scattering From One- and Two-Phonon States of BaTiO3. D. L. Rousseau & S.P.S. Porto Phys. Rev. Lett. 20, 1354-1357 (1968). 4. Raman Spectrum of Crystalline Sodium Nitrate. D. L. Rousseau, R. E. Miller & G. E. Leroi J. Chem. Phys. 48, 3409-3413 (1968). 3. Laser Photochemistry. D. L. Rousseau Diss. Abstracts 291, 78-B (1968). 2. Laser Chemistry. D. L. Rousseau J. Chem. Educ. 43, 566-570 (1966). 1. Two-Photon Induced Chemical Reaction in AgCl. D. L. Rousseau, G. E. Leroi & G. L. Link J. Chem. Phys. 42, 4048-4049 (1965).
 

More Information About Dr. Denis Rousseau

Rousseau - Home page

Material in this section is provided by individual faculty members who are solely responsible for its accuracy and content.

Contact

Albert Einstein College of Medicine
Jack and Pearl Resnick Campus
1300 Morris Park Avenue
Ullmann Building, Room 325
Bronx, NY 10461

Tel: 718.430.3592
Fax: 718.430.8808
denis.rousseau@einstein.yu.edu

 
Pubmed Search
Collexis Research Profiles
Einstein Research Profiles (ERP) is one of the innovative technologies to create collaborative bridges within and across the entire bench-to-bedside-to-population spectrum of research. The ERP website has been developed in partnership with Collexis to give investigators easy access to PubMed publications, coauthor networks, information about NIH grants, and research networks.