HR job title
- Associate Professor
- Contact Info
Barondeau, David Associate Professor
Positions
- Associate Professor, Chemistry, College of Arts and Sciences
Our group conducts research on Fe-S cluster biogenesis.
- Overview
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- Research
- Teaching
- Works By Students
- Background
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Overview
Publications
selected publications
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academic article
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Zulkifli, M., Spelbring, A. N., Zhang, Y., Soma, S., Chen, S. i., Li, L., ... Gohil, V. M.
(2023).
FDX1-dependent and independent mechanisms of elesclomol-mediated intracellular copper delivery. 120(10), e2216722120.
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Lin, C., Oney-Hawthorne, S. D., Kuo, S., Barondeau, D. P., & Russell, D. H.
(2022).
Mechanistic Insights into IscU Conformation Regulation for Fe-S Cluster Biogenesis Revealed by Variable Temperature Electrospray Ionization Native Ion Mobility Mass Spectrometry. Biochemistry.
61(23), 2733-2741.
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McCabe, J. W., Shirzadeh, M., Walker, T. E., Lin, C., Jones, B. J., Wysocki, V. H., ... Russell, D. H.
(2021).
Variable-Temperature Electrospray Ionization for Temperature-Dependent Folding/Refolding Reactions of Proteins and Ligand Binding. Analytical Chemistry.
93(18), 6924-6931.
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Lin, C., McCabe, J. W., Russell, D. H., & Barondeau, D. P.
(2020).
Molecular Mechanism of ISC Iron-Sulfur Cluster Biogenesis Revealed by High-Resolution Native Mass Spectrometry. Journal of the American Chemical Society.
142(13), 6018-6029.
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Patra, S., & Barondeau, D. P.
(2019).
Mechanism of activation of the human cysteine desulfurase complex by frataxin. Proceedings of the National Academy of Sciences of the United States of America.
116(39), 19421-19430.
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Hogancamp, T. N., Cory, S. A., Barondeau, D. P., & Raushel, F. M.
(2019).
Structure and Chemical Reaction Mechanism of LigU, an Enzyme That Catalyzes an Allylic Isomerization in the Bacterial Degradation of Lignin. Biochemistry.
58(33), 3494-3503.
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Das, D., Patra, S., Bridwell-Rabb, J., & Barondeau, D. P.
(2019).
Mechanism of frataxin "bypass" in human iron-sulfur cluster biosynthesis with implications for Friedreich's ataxia. 294(23), 9276-9284.
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Ast, T., Meisel, J. D., Patra, S., Wang, H., Grange, R., Kim, S. H., ... Mootha, V. K.
(2019).
Hypoxia Rescues Frataxin Loss by Restoring Iron Sulfur Cluster Biogenesis. Cell.
177(6), 1507-1521.e16.
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Cory, S. A., Van Vranken, J. G., Brignole, E. J., Patra, S., Winge, D. R., Drennan, C. L., Rutter, J., & Barondeau, D. P.
(2017).
Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions. Proceedings of the National Academy of Sciences of the United States of America.
114(27), E5325-E5334.
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Vranish, J. N., Das, D., & Barondeau, D. P.
(2016).
Real-Time Kinetic Probes Support Monothiol Glutaredoxins As Intermediate Carriers in Fe-S Cluster Biosynthetic Pathways. ACS Chemical Biology.
11(11), 3114-3121.
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Fox, N. G., Das, D., Chakrabarti, M., Lindahl, P. A., & Barondeau, D. P.
(2015).
Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex. Biochemistry.
54(25), 3880-3889.
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Fox, N. G., Chakrabarti, M., McCormick, S. P., Lindahl, P. A., & Barondeau, D. P.
(2015).
The Human Iron-Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor Molecules. Biochemistry.
54(25), 3871-3879.
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Vranish, J. N., Russell, W. K., Yu, L. E., Cox, R. M., Russell, D. H., & Barondeau, D. P.
(2015).
Fluorescent probes for tracking the transfer of iron-sulfur cluster and other metal cofactors in biosynthetic reaction pathways. Journal of the American Chemical Society.
137(1), 390-398.
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Bridwell-Rabb, J., Fox, N. G., Tsai, C., Winn, A. M., & Barondeau, D. P.
(2014).
Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry. Biochemistry.
53(30), 4904-4913.
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Meier, M. M., Rajendran, C., Malisi, C., Fox, N. G., Xu, C., Schlee, S., ... Raushel, F. M.
(2013).
Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template. Journal of the American Chemical Society.
135(31), 11670-11677.
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Tsai, P., Fox, N., Bigley, A. N., Harvey, S. P., Barondeau, D. P., & Raushel, F. M.
(2012).
Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents. Biochemistry.
51(32), 6463-6475.
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Bridwell-Rabb, J., Iannuzzi, C., Pastore, A., & Barondeau, D. P.
(2012).
Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis. Biochemistry.
51(12), 2506-2514.
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Bridwell-Rabb, J., Winn, A. M., & Barondeau, D. P.
(2011).
Structure-function analysis of Friedreich's ataxia mutants reveals determinants of frataxin binding and activation of the Fe-S assembly complex. Biochemistry.
50(33), 7265-7274.
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Tsai, C., Bridwell-Rabb, J., & Barondeau, D. P.
(2011).
Friedreich's ataxia variants I154F and W155R diminish frataxin-based activation of the iron-sulfur cluster assembly complex. Biochemistry.
50(29), 6478-6487.
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Tsai, C., & Barondeau, D. P.
(2010).
Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex. Biochemistry.
49(43), 9132-9139.
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Wood, T. L., Bridwell-Rabb, J., Kim, Y., Gao, T., Chang, Y., LiWang, A., Barondeau, D. P., & Golden, S. S.
(2010).
The KaiA protein of the cyanobacterial circadian oscillator is modulated by a redox-active cofactor. Proceedings of the National Academy of Sciences of the United States of America.
107(13), 5804-5809.
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Cummings, J. A., Nguyen, T. T., Fedorov, A. A., Kolb, P., Xu, C., Fedorov, E. V., ... Raushel, F. M.
(2010).
Structure, mechanism, and substrate profile for Sco3058: the closest bacterial homologue to human renal dipeptidase . Biochemistry.
49(3), 611-622.
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Shin, D. S., Didonato, M., Barondeau, D. P., Hura, G. L., Hitomi, C., Berglund, J. A., ... Tainer, J. A.
(2009).
Superoxide dismutase from the eukaryotic thermophile Alvinella pompejana: structures, stability, mechanism, and insights into amyotrophic lateral sclerosis. Journal of Molecular Biology.
385(5), 1534-1555.
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Barondeau, D. P., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2007).
The case of the missing ring: radical cleavage of a carbon-carbon bond and implications for GFP chromophore biosynthesis. Journal of the American Chemical Society.
129(11), 3118-3126.
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Barondeau, D. P., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2006).
Understanding GFP posttranslational chemistry: structures of designed variants that achieve backbone fragmentation, hydrolysis, and decarboxylation. Journal of the American Chemical Society.
128(14), 4685-4693.
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Barondeau, D. P., Tainer, J. A., & Getzoff, E. D.
(2006).
Structural evidence for an enolate intermediate in GFP fluorophore biosynthesis. Journal of the American Chemical Society.
128(10), 3166-3168.
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Wood, T. I., Barondeau, D. P., Hitomi, C., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2005).
Defining the role of arginine 96 in green fluorescent protein fluorophore biosynthesis. Biochemistry.
44(49), 16211-16220.
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Barondeau, D. P., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2005).
Understanding GFP chromophore biosynthesis: controlling backbone cyclization and modifying post-translational chemistry. Biochemistry.
44(6), 1960-1970.
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Barondeau, D. P., & Getzoff, E. D.
(2004).
Structural insights into protein-metal ion partnerships. Current Opinion in Structural Biology.
14(6), 765-774.
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Barondeau, D. P., Kassmann, C. J., Bruns, C. K., Tainer, J. A., & Getzoff, E. D.
(2004).
Nickel superoxide dismutase structure and mechanism. Biochemistry.
43(25), 8038-8047.
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Barondeau, D. P., Putnam, C. D., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2003).
Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures. Proceedings of the National Academy of Sciences of the United States of America.
100(21), 12111-12116.
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Barondeau, D. P., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2002).
Structural chemistry of a green fluorescent protein Zn biosensor. Journal of the American Chemical Society.
124(14), 3522-3524.
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Barondeau, D. P., Hellinga, H. W., Pique, M. E., Tainer, J. A., & Getzoff, E. D.
(1999).
The rational design of green fluorescent protein metallomutants. Journal of Inorganic Biochemistry.
74(1-4), 75-75.
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Barondeau, D. P., & Lindahl, P. A.
(1997).
Methylation of carbon monoxide dehydrogenase from Clostridium thermoaceticum and mechanism of acetyl coenzyme A synthesis. Journal of the American Chemical Society.
119(17), 3959-3970.
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Barondeau, D. P., Xia, J. Q., Russell, W. K., & Lindahl, P. A.
(1996).
Unraveling the structures and functions of the unusual Ni-Fe-S clusters in carbon monoxide dehydrogenase. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY.
211, 3-INOR.
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BARONDEAU, D. P., ROBERTS, L. M., & LINDAHL, P. A.
(1994).
STABILITY OF THE NI-C STATE AND OXIDATIVE TITRATIONS OF DESULFOVIBRIO-GIGAS HYDROGENASE MONITORED BY EPR AND ELECTRONIC ABSORPTION SPECTROSCOPIES. Journal of the American Chemical Society.
116(8), 3442-3448.
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Zulkifli, M., Spelbring, A. N., Zhang, Y., Soma, S., Chen, S. i., Li, L., ... Gohil, V. M.
(2023).
FDX1-dependent and independent mechanisms of elesclomol-mediated intracellular copper delivery. 120(10), e2216722120.
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conference paper
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Cory, S. A., Van Vranken, J. G., Brignole, E. J., Patra, S., Winge, D. R., Drennan, C. L., Rutter, J., & Barondeau, D. P.
(2018).
Structure of the human Fe-S cluster assembly sub-complex: implications in Friedreich's ataxia and primary metabolism. Acta Crystallographica Section A: Foundations and Advances.
A80-A80.
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Cory, S. A., Van Vranken, J. G., Brignole, E. J., Patra, S., Winge, D. R., Drennan, C. L., Rutter, J., & Barondeau, D. P.
(2017).
Structure of human Fe-S assembly sub-complex. Acta Crystallographica Section A: Foundations and Advances.
A113-A113.
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Senn, K., Cory, S., & Barondeau, D.
(2016).
Hydroxyl radical footprinting of the human Fe-S cluster assembly complex. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY.
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James, E. S., Fox, N., Vranish, J., & Barondeau, D.
(2014).
Elucidating the role of IscX in bacterial Fe-S cluster assembly. ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY.
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Wood, T. I., Barondeau, D. P., Hitomi, C., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2004).
Mechanism for GFP fluorophore synthesis: Electrostatic role of arginine 96 in backbone cyclization. Protein Science.
153-154.
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Barondeau, D. P., Kassman, C. J., Bruns, C. K., Tainer, J. A., & Getzoff, E. D.
(2004).
Nickel superoxide dismutase structure and mechanism. Protein Science.
192-192.
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Barondeau, D. P., Putnam, C. D., Wood, T. I., Kassmann, C. J., Tainer, J. A., & Getzoff, E. D.
(2004).
Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures and modified post-translational chemistry. Protein Science.
153-153.
-
Cory, S. A., Van Vranken, J. G., Brignole, E. J., Patra, S., Winge, D. R., Drennan, C. L., Rutter, J., & Barondeau, D. P.
(2018).
Structure of the human Fe-S cluster assembly sub-complex: implications in Friedreich's ataxia and primary metabolism. Acta Crystallographica Section A: Foundations and Advances.
A80-A80.
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institutional repository document
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Cory, S., Lin, C., Havens, S., Patra, S., Putnam, C., Shirzadeh, M., Russell, D., & Barondeau, D.
(2024).
Frataxin Traps Low Abundance Quaternary Structure to Stimulate Human Fe-S Cluster Biosynthesis
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Patra, S., Lin, C., Ghosh, M. K., Havens, S. M., Cory, S. A., Russell, D. H., & Barondeau, D. P.
(2020).
Recapitulating the frataxin activation mechanism in an engineered bacterial cysteine desulfurase supports the architectural switch model
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Cory, S., Lin, C., Havens, S., Patra, S., Putnam, C., Shirzadeh, M., Russell, D., & Barondeau, D.
(2024).
Frataxin Traps Low Abundance Quaternary Structure to Stimulate Human Fe-S Cluster Biosynthesis
Research
principal investigator on
- Structure And Mechanism Of The Human Fe-S Cluster Assembly Complex awarded by National Institutes of Health - (Bethesda, Maryland, United States) 2017 - 2021
- Macromolecular juggling for a prokaryotic Fe-S assembly system awarded by National Science Foundation - (Arlington, Virginia, United States) 2015 - 2018
- Structure and Mechanism of the Human FE-S Cluster Assembly Complex awarded by National Institutes of Health - (Bethesda, Maryland, United States) 2011 - 2017
Teaching
teaching activities
- BICH491 Hnr-research Instructor
- BICH685 Directed Studies Instructor
- BICH691 Research Instructor
- CHEM119 Fund Of Chemistry I Instructor
- CHEM120 Fund Of Chemistry Ii Instructor
- CHEM289 Sptp: General Chem Ii Lec Instructor
- CHEM491 Hnr-research Instructor
- CHEM628 Coord & Bioinorg Chem Instructor
- CHEM681 Seminar Instructor
- CHEM685 Directed Studies Instructor
- CHEM689 Sptp: Chem Biol Grad Seminar Instructor
- CHEM690 Theory Of Chem Resrch Instructor
- CHEM691 Research Instructor
- GENE491 Hnr-research Instructor
Works By Students
chaired theses and dissertations
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Choi, Hyeran (2016-07). Investigating the Enzymology of Fe-S Cluster Assembly in the Bacterial ISC System.
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Das, Deepika (2018-05). Mechanistic Analysis of Cluster Transfer to Apo-acceptors in ISC Pathway.
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Fox, Nicholas G (2014-06). A Biophysical Approach to Investigate the Human Fe-S Cluster Assembly Pathway.
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Levy, Michaella J (2014-06). Protein-Protein Interactions of the Human Iron Sulfur Cluster Biosynthesis Complex.
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Martin Jr., Darrell Wayne (2016-08). A Class of Its Own: Function-Discovery of HydY, A Novel Class of [FeFe]-Hydrogenases.
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Patra, Shachin (2018-06). Mechanistic Analysis of the Role of Frataxin in Bacterial and Eukaryotic Fe-S Cluster Biosynthetic Pathways.
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Patra, Shachin (2018-08). Mechanistic Analysis of the Role of Frataxin in Bacterial and Eukaryotic Fe-S Cluster Biosynthetic Pathways.
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Rabb, Jennifer (2012-07). Frataxin (FXN) Based Regulation of the Iron-Sulfur Cluster Assembly Complex.
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Thorstad, Melissa (2013-05). Functional Characterization and Surface Mapping of Frataxin (FXN) Interactions with the Fe-S Cluster Assembly Complex.
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Tsai, Chi-Lin (2012-07). Structural and Functional Studies on Human Mitochondrial Iron-Sulfur Cluster Biosynthesis.
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Vranish, James Nicholas (2015-04). Development of Fluorescent Reporters for Monitoring Fe-S Cluster Transfer Reactions and Discerning the Role of Glutaredoxin Proteins in Fe-S Cluster Assembly.
Background
education and training
Contact
first name
- David
has last name
- Barondeau
mailing address
-
Texas A&M University
Chemistry Department
3255 TAMU
College Station, TX 77843-3255
USA
Other
- barondeau@tamu.edu