Publications

Bennett, Z. D.; Brunold, T. C. “Non-Standard Amino Acid Incorporation into Thiol Dioxygenases”, Methods in Enzymology, Academic Press 2024, 703, 121-145. Invited article.

Miller, J. R.; Schorrenberg, E. C.; Aschenbrener, C.; Fox, B. G.; Brunold, T. C. “Kinetic and Spectroscopic Investigation of the Y157F and C93G/Y157F Variants of Cysteine Dioxygenase: Dissecting the Roles of the Second-Sphere Residues C93 and Y157”,  Biochemistry 2024, 63, 1684-1696.

Killian, M. M.; Brophy, M. B.; Nolan. E. M.; Brunold, T. C. “Spectroscopic and Computational Investigations of Cobalt(II) Binding to the Innate Immune Protein Human Calprotectin”, J. Biol. Inorg. Chem. 2024, 29, 127-137.

Elmendorf, L. G.; Brunold, T. C. “Vibronic Coupling in Vitamin B12: A Combined Spectroscopic and Computational Study”, Inorg. Chem. 2023, 62, 12762–12772. Selected for cover art.

Schultz, R. L.; Sabat, G.;  Fox, B. G.; Brunold, T. C. “A Single DNA Point Mutation Leads to the Formation of a Cysteine–Tyrosine Crosslink in the Cysteine Dioxygenase from Bacillus subtilis”, Biochemistry 2023, 62, 1964–1975.

Miller, J. R.; Brunold, T. C. “Spectroscopic Analysis of the Mammalian Enzyme Cysteine Dioxygenase”, Methods in Enzymology, Academic Press 2023, 682, 101–135. Invited article.

Fernandez, R. L.; Juntunen, N. D.; Brunold, T. C. “Differences in the Second Coordination Sphere Tailor the Substrate Specificity and Reactivity of Thiol Dioxygenases”, Acc. Chem. Res. 2022, 55, 2480–2490.

Elmendorf, L. G.; Brunold, T. C. “Electronic Structure Studies of Free and Enzyme-Bound B₁₂ Species by Magnetic Circular Dichroism and Complementary Spectroscopic Techniques”, in Marsh, E. N. G., Ed.; Methods in Enzymology, Academic Press 2022, 669, 333–365. Invited article.

Greenhalgh, E. D.; Kincannon, W.; Bandarian, V.; Brunold, T. C. “Spectroscopic and Computational Investigation of the Epoxyqueuosine Reductase QueG Reveals Intriguing Similarities with the Reductive Dehalogenase PceA”, Biochemistry 2022, 61, 195–205.

Fernandez, R. L.; Elmendorf, L. D.; Smith, R. W.; Bingman, C. A.; Fox, B. G.; Brunold, T. C. “Crystal Structure of Cysteamine Dioxygenase Reveals the Origin of the Large Substrate Scope of this Vital Mammalian Enzyme”, Biochemistry 2021, 60, 3728–3737.

Greenhalgh, E. D.; Brunold, T. C. “Biorelevant Chemistry of Cobalamin”, in Constable, E. C.; Parkin, G.; Que, L., Jr., Eds.; Comprehensive Coordination Chemistry III, Elsevier 2021, 812–824. Invited article.

Fernandez, R. L.; Juntunen, N. D.; Fox, B. G.; Brunold, T. C. “Spectroscopic Investigation of Iron(III) Cysteamine Dioxygenase in the Presence of Substrate (Analogs): Implications for the Nature of Substrate-Bound Reaction Intermediates”, J. Biol. Inorg. Chem. 2021, 26, 947–955.

Greenhalgh, E. D.; Kunze, C.; Schubert, T.; Diekert, G.; Brunold, T. C. “A Spectroscopically Validated Computational Investigation of Viable Reaction Intermediates in the Catalytic Cycle of the Reductive Dehalogenase PceA”, Biochemistry 2021, 60, 2022–2032.

Costa, F. G.; Greenhalgh, E. D.; Brunold, T. C.; Escalante-Semerena, J. C. “Mutational and Functional Analyses of Substrate Binding and Catalysis of the Listeria monocytogenes EutT ATP:Co(I)rrinoid Adenosyltransferase”, Biochemistry 2020, 59, 1124–1136.

Fernandez, R. L.; Dillon, S. L.; Stipanuk, M. H.; Fox, B. G.; Brunold, T. C. “Spectroscopic Investigation of Cysteamine Dioxygenase”, Biochemistry 2020, 59, 2450–2458.

Li, Z.; Greenhalgh, E. D.; Twahir, U. T.; Kallon, A.; Ruetz, M.; Warncke, K.; Brunold, T. C.; Banerjee, R. “Chlorocob(II)alamin Formation Which Enhances the Thiol Oxidase Activity of the B₁₂-Trafficking Protein CblC”, Inorg. Chem. 2020, 59, 16065–16072.

Fischer, A.; Miller, J.; Jodts, R.; Ekanayake, D.; Lindeman, S.; Brunold, T. C.; Fiedler, A. T. “Spectroscopic and Computational Comparisons of Thiolate-Ligated Ferric Nonheme Complexes to Cysteine Dioxygenase:  Second-Sphere Effects On Substrate (Analogue) Positioning”, Inorg. Chem. 2019, 58, 16487–16499.

Tavares, N. K.; Stracey, N.; Brunold, T. C.; Escalante-Semerena, J. C. “The L-Thr Kinase/L-Thr-Phosphate Decarboxylase (CobD) Enzyme from Methanosarcina mazei Go1 Contains Metallocenters Needed for Optimal Activity”, Biochemistry 2019, 58, 3260–3279.

Handali, J. D.; Sunden, K. F.; Thompson, B. J.; Neff-Mallon, N. A.; Kaufman, E. M.; Brunold, T. C.; Wright, J. C. “Three Dimensional Triply Resonant Sum Frequency Spectroscopy Reveals Vibronic Coupling in Cobalamins: Towards a Probe of Reaction Coordinates”, J. Phys. Chem. A 2018, 122, 9031–9042.

Campanello, G. C.; Ruetz, M.; Dodge, G. J.; Gouda, H.; Gupta, A.; Twahir, U. T.; Killian, M. M.; Watkins, D.; Rosenblatt, D. S.; Brunold, T. C.; Warncke, K.; Smith, J. L.; Banerjee, R. “Sacrificial Cobalt-carbon Bond Homolysis in Coenzyme B₁₂ as a Cofactor Conservation Strategy”, J. Am. Chem. Soc. 2018, 140, 13205–13208.

Huang, H.-T.; Dillon, S.; Ryan, K. C.; Campecino, J. O.; Watkins, O. E.; Cabelli, D. E.; Brunold, T. C.; Maroney^, M. J. “The Role of Mixed Amine/Amide Ligation in Nickel Superoxide Dismutase”, Inorg, Chem. 2018, 57, 12521–12535.

Stracey, N. G.; Costa, F. G.; Escalante-Semerena, J. C.; Brunold, T. C. “Spectroscopic Study of the EutT Adenosyltransferase from Listeria monocytogenes: Evidence for the Formation of a Four-Coordinate Cob(II)alamin Intermediate”, Biochemistry 2018, 57, 5088–5095.

Corcos, A. R.; Roy, M. D.; Killian, M. M.; Dillon, S.; Brunold, T. C.; Berry, J. F. “Electronic Structure of Anilinopyridinate-Supported Ru₂⁵⁺ Paddlewheel Compounds”, Inorg. Chem. 2017, 56, 14662–14670.

Wang, P.; Killian, M. M.; Saber, M. R.; Qiu, T.; Yap, G. P. A.; Popescu, C. V.; Rosenthal, J.; Dunbar, K. R; Brunold, T. C.; Riordan C. G. “Electronic, Magnetic, and Redox Properties and O₂ Reactivity of Iron(II) and Nickel(II) o-Semiquinonate Complexes of a Tris(thioether) Ligand: Uncovering the Intradiol Cleaving Reactivity of an Iron(II) o-Semiquinonate Complex”, Inorg. Chem. 2017, 56, 10481–10495.

Acheson, J. F.; Bailey, L. J.; Brunold, T. C.; Fox, B. G. “In-crystal Reaction Cycle of a Toluene Bound Diiron Hydroxylase”, Nature 2017, 544, 191-195.

Li, Z.; Shanmuganathan, A.; Ruetz, M.; Yamada, K.; Lesniak, N. A.; Kräutler, B.; Brunold, T. C.; Koutmos^, M.; Banerjee, R. “Coordination Chemistry Controls the Thiol Oxidase Activity of the B₁₂ Trafficking Protein CblC”, J. Biol. Chem. 2017, 292, 9733–9744.

Pallares, I. G.; Moore, T. C.; Escalante-Semerena, J. C.; Brunold, T. C. “Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Evidence of a Tetrahedrally Coordinated Divalent Transition Metal Cofactor with Cysteine Ligation”, Biochemistry 2017, 56, 364–375.

Fischer, A. A.; Stracey, N.; Lindeman, S. V.; Brunold, T. C.; Fiedler, A. T. “Synthesis, X-ray Structures, Electronic Properties, and O₂/NO Reactivities of Thiol Dioxygenase Active-Site Models”, Inorg. Chem., 2016, 55, 11839–11853.

Bostelaar, T.; Vitvitsky, V.; Kumutima, J.; Lewis, B. E.; Yadav, P. K.; Brunold, T. C.; Filipovic, M.; Lehnert, N.; Stemmler, T. L.; Banerjee, R. “Hydrogen Sulfide Oxidation by Myoglobin”, J. Am. Chem. Soc., 2016, 138, 8476–8488.

Park, K.; Mera, P.; Escalante-Semerena, J. C.; Brunold, T. C. “Resonance Raman Spectroscopic Study of the Interaction between Co(II)rrinoids and the ATP:Corrinoid Adenosyltransferase PduO from Lactobacillus reuteri”, J. Biol. Inorg. Chem. 2016, 21, 669–681.

Pallares, I. G.; Moore, T. C.; Escalante-Semerena,J. C.; Brunold, T. C. “Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Mechanism of Four‑coordinate Co(II)Cbl Formation”, J. Am. Chem. Soc. 2016, 138, 3694–3704.

Park, K.; Mera, P.; Moore, T. C.; Escalante-Semerena, J. C.; Brunold, T. C. “Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:CoIrrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co^IIrrinoids”, Angew. Chem. Int. Ed. 2015, 54, 7158–7161.

Conrad, K. S.; Jordan, C. D.; Brown, K. L.; Brunold, T. C. “Spectroscopic and Computational Studies of Cobalamin Species with Variable Lower Axial Ligation: Implications for the Mechanism of Co–C Bond Activation by Class I Cobalamin-Dependent Isomerases”, Inorg. Chem. 2015, 54, 3736–3747.

Blaesi, E. J.; Fox. B. G.; Brunold, T. C. “Spectroscopic and Computational Investigation of the H155A Variant of Cysteine Dioxygenase: Geometric and Electronic Consequences of a Third-Sphere Amino Acid Substitution”, Biochemistry 2015, 54, 2874–2884.

Broering, E.; Dillon, S.; Gale, E.; Steiner, R.; Telser, J.; Brunold, T.C.; Harrop, T. “Accessing Ni(III)-Thiolate versus Ni(II)-Thiyl Bonding in a Family of Ni-N₂S₂ Synthetic Models of NiSOD”, Inorg. Chem. 2015, 54, 3815–3828.

Ryan, K. C.; Guce, A. I.; Johnson, O. E.; Brunold, T. C.; Cabelli, D. E.; Garman, S. C.; Maroney, M. J. “Nickel Superoxide Dismutase: Structural and Functional Roles of His1 and Its H-Bonding Network”, Biochemistry 2015, 54, 1016-1027.

Pallares, I. G.; Moore, T. C.; Escalante-Semerena, J. C.; Brunold, T. C. “Spectroscopic Studies of the Salmonella enterica Adenosyltransferase Enzyme SeCobA: Molecular-Level Insight into the Mechanism of Substrate Cob(II)alamin Activation”, Biochemistry 2014, 53, 7969–7982.

Blaesi, E. J.; Fox. B. G.; Brunold, T. C. “Spectroscopic and Computational Investigation of Iron(III) Cysteine Dioxygenase: Implications for the Nature of the Putative Superoxo-Fe(III) Intermediate”, Biochemistry 2014, 53, 5759-5770.

Ryland. B. L.; McCann, S. D.; Brunold, T. C.; Stahl, S. S. “Mechanism of Alcohol Oxidation Mediated by Copper(II) and Nitroxyl Radicals”, J. Am. Chem. Soc. 2014, 136, 12166–12173.

Pallares, I. G.; Brunold, T. C. “Spectral and Electronic Properties of Nitrosylcobalamin”, Inorg. Chem. 2014, 53, 7676–7691.

Blaesi, E. J.; Gardner, J. D.; Fox. B. G.; Brunold, T. C. “Spectroscopic and Computational Characterization of the NO Adduct of Substrate-Bound Fe(II) Cysteine Dioxygenase: Insights into the Mechanism of O₂ Activation”, Biochemistry 2013, 52, 6040-6051.

Gutman, C. T.; Guzei, I. A.; Brunold, T. C. “Structural, Spectroscopic, and Computational Characterization of the Azide Adduct of Fe^III(2,6-diacetylpyridinebis(semioxamazide)), a Functional Analogue of Iron Superoxide Dismutase“, Inorg. Chem. 2013, 52, 8909–8918.

Jackson, T. A.; Gutman, C. T.; Maliekal, J.; Miller, A.-F.; Brunold, T. C. “Geometric and Electronic Structures of Manganese-Substituted Iron Superoxide Dismutase“, Inorg. Chem. 2013, 52, 3356–3367.

Park, K.; Brunold, T. C. “Combined Spectroscopic and Computational Analysis of the Vibrational  Properties of Vitamin B₁₂ in its Co³⁺, Co²⁺ and Co¹⁺ Oxidation States“, J. Phys. Chem. B 2013, 117, 5397–5410.

Gutman, C. T.; Brunold, T. C. “Spectroscopic and Computational Studies of a Small-Molecule Functional Mimic of Iron Superoxide Dismutase, Iron 2,6-Diacetylpyridinebis(semioxamazide)“, Inorg. Chem. 2012, 51, 12729–12737.

King, A. E.; Ryland, B. L.; Brunold, T. C.; Stahl, S. S. “Kinetic and Spectroscopic Studies of Aerobic Copper(II)-Catalyzed Methoxylation of Arylboronic Esters and Insights into Aryl Transmetalation to Copper(II)“, Organometallics 2012, 31, 7948–7957.

Reig, A. J.; Conrad, K. S.; Brunold, T. C. “Combined Quantum Mechanics/Molecular Mechanics Studies of Vitamin B₁₂ Derivatives:  Geometric and Electronic Structures of Cobinamides”, Inorg. Chem. 2012, 51, 2867–2879.

Park, K.; Mera, P.; Escalante-Semerena, J. C.; Brunold, T. C. “Spectroscopic Characterization of Active-site Variants of the PduO-type ATP:Corrinoid Adenosyltransferase from Lactobacillus reuteri: Insights into the Mechanism of Four-coordinate Co(II)corrinoid Formation”, Inorg. Chem. 2012, 51, 4482–4494.

Fleischhacker, A. S.; Stubna, A.; Hsueh, K.-L.; Guo, Y.; Teter, S. J.; Rose, J. C.; Brunold, T. C.; Markley, J. L.; Münck, E. Kiley, P. J. “Characterization of the [2Fe-2S] cluster of the Escherichia coli transcription factor IscR”, Biochemistry 2012, 51, 4453-4462.

Conrad, K. S.; Brunold, T. C. “Spectroscopic and Computational Studies of Glutathionylcobalamin: Nature of Co–S Bonding and Comparison to Co–C bonding in Coenzyme B₁₂”, Inorg. Chem. 2011, 70, 6313–6324.

Gardner, J. D.; Pierce, B. S.; Fox. B. G.; Brunold, T. C. “Spectroscopic and Computational Characterization of Substrate-Bound Mouse Cysteine Dioxygenase: Nature of the Ferrous and Ferric Cysteine Adducts and Mechanistic Implications”, Biochemistry 2010, 49, 6033-6041.

Van Heuvelen, K. M.; Cho, J.; Dingee, T.; Riordan, C. G.; Brunold, T. C. “Spectroscopic and Computational Studies of a Series of High-Spin Ni(II) Thiolate Complexes”, Inorg. Chem. 2010, 69, 6535-6544.

Gardner, J. D.; Li, Y.; Ragsdale, S. W.; Brunold, T. C. “Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2”, J. Biol. Inorg. Chem. 2010, 15, 1117-1127.

Ryan, K. C.; Johnson, O. E.; Cabelli, D. E.; Brunold, T. C.; Maroney, M. J. “Nickel Superoxide Dismutase: Structural and Functional Roles of Cys2 and Cys6”, J. Biol. Inorg. Chem. 2010, 15, 795-807.

Johnson, O. E.; Ryan, K. C.; Maroney, M. J.; Brunold, T. C. “Spectroscopic and Computational Investigation of three Cys-to-Ser Mutants of Nickel Superoxide Dismutase: Insight into the Roles Played by the Cys2 and Cys6 Active-Site Residues”, J. Biol. Inorg. Chem. 2010, 15, 777-793.

Van Heuvelen, K. M.; Cho, J.; Riordan, C. G.; Brunold, T. C. “Spectroscopic and Computational Studies of a m-h²:h²-Disulfido-Bridged Dinickel(II) Species, [{(PhTt^tBu)Ni}₂(m-h²:h²-S₂)]: Comparison of Side-on Disulfido and Peroxo Bonding in (Ni²⁺)₂ and (Cu²⁺)₂ Species”, Inorg. Chem. 2010, 49, 3113-3120.

Van Heuvelen, K. M.; Kieber-Emmons, M. T.; Riordan, C. G.; Brunold, T. C. “Spectroscopic and Computational Studies of a Trans-μ-1,2-Disulfido-Bridged Dinickel Species, [{(tmc)Ni}₂(S₂)](OTf)₂: Comparison of End-on Disulfido and Peroxo Bonding in (Ni²⁺)₂ and (Cu²⁺)₂ Species”, Inorg. Chem. 2010, 49, 3104-3112.

Brunold, T. C. “Computational Studies of the B₁₂ Cofactors and their Interaction with Enzyme Active Sites”, in Solomon, E. I.; Scott; R. A.; King, R. B., Eds.; “Computational Inorganic and Bioinorganic Chemistry”, John Wiley & Sons, 2009. Invited article.

Liptak, M. D.; Van Heuvelen, K. M.; Brunold, T. C. “Computational Studies of Bioorganometallic Enzymes and Cofactors”, in Sigel, A.; Sigel; H.; Sigel, R. K. O., Eds.; “Metal Ions in Life Sciences”, The Royal Society of Chemistry, Cambridge, UK, 2009, 6, 417-460. Invited article.

Liptak, M. D.; Fleischhacker, A. S.; Matthews, R. G.; Telser, J.; Brunold, T. C. “Spectroscopic and Computational Characterization of the Base-off Forms of Cob(II)alamin”, J. Phys. Chem. B 2009, 113, 5245-5254

King, A. E.; Brunold, T. C.; Stahl, S. S. “Mechanistic Study of Copper-Catalyzed Aerobic Oxidative Coupling of Arylboronic Esters and Methanol: Insights into an Organometallic Oxidase Reaction”, J. Am. Chem. Soc. 2009, 131, 5044-5045.

Kieber-Emmons, M. T.; Van Heuvelen, K. M.; Brunold, T. C.; Riordan, C. G. “Synthesis and Spectroscopic Identification of a µ-1,2-Disulfidodinickel Complex”, J. Am. Chem. Soc. 2009, 131, 440-441.

Brunold, T. C.; Conrad, K.; Liptak, M. D.; Park, K. “Spectroscopically Validated Density Functional Theory Studies of the B₁₂ Cofactors and their Interactions with Enzyme Active Sites”, Coord. Chem. Rev. 2009, 253, 779-794. Invited article.

Liptak, M. D.; Datta, S.; Matthews, R.; Brunold, T. C. “Spectroscopic Study of the Cobalamin-Dependent Methionine Synthase in the Activation Conformation: Effects of the Y1139 Residue and S-Adenosylmethionine on the B₁₂ Cofactor”, J. Am. Chem. Soc. 2008, 130, 16374-16381.

Grove, L. E.; Brunold, T. C. “Second-Sphere Tuning of the Metal Ion Reduction Potentials in Iron and Manganese Superoxide Dismutases”, Comments on Inorganic Chemistry, 2008, 29, 134-168. Invited article.

Cho, J.; Van Heuvelen, K. M.; Yap, G. P. A.; Brunold, T. C.; Riordan, C. G. “New Synthetic Routes to a Disulfidodinickel(II) Complex: Characterization and Reactivity of a Ni₂(m-h²:h²-S₂) Core”, Inorg. Chem. 2008, 47, 3931-3933.

Park, K.; Mera, P.; Escalante-Semerena, J. C.; Brunold, T. C. “Kinetic and Spectroscopic Studies of the ATP:Corrinoid Adenosyltransferase PduO from Lactobacillus reuteri: Insights into Substrate Specificity and Mechanism of Co(II)corrinoid Reduction”, Biochemistry 2008, 47, 9007-9015.

St. Maurice, M.; Mera, P; Park, K; Brunold, T. C.; Escalante-Semerena, J. C.; Rayment, I. “Structural Characterization of a Human-Type Corrinoid Adenosyltransferase Confirms that Coenzyme B₁₂ is Synthesized Through a Four-Coordinate Intermediate” Biochemistry 2008, 47, 5755-5766.

Grove, L. E.; Hallman, J. K.; Emerson, J. P.; Halfen, J. A.; Brunold, T. C. “Synthesis, X-ray Crystallographic Characterization, and Electronic Structure Studies of a Di-Azide Iron(III) Complex: Implications for the Azide Adducts of Iron(III) Superoxide Dismutase”, Inorg. Chem. 2008, 47, 5762-5774.

Grove, L. E.; Xie, J.; Yikilmaz, E.; Karapetyan, A.; Miller, A.-F; Brunold, T. C. “Spectroscopic and Computational Insights into Second-Sphere Amino-Acid Tuning of Substrate Analogue/Active-Site Interactions in Iron(III) Superoxide Dismutase”, Inorg. Chem. 2008, 47, 3993-4004.

Grove, L. E.; Xie, J.; Yikilmaz, E.; Miller, A.-F; Brunold, T. C. “Spectroscopic and Computational Insights into Second-Sphere Contributions to Redox Tuning in Escherichia coli Iron Superoxide Dismutase”, Inorg. Chem. 2008, 47, 3978-3992.

Brunold, T. C. “Synthetic Iron-Oxo “Diamond Core” Mimics Structure of Key Intermediate in Methane Monooxygenase Catalytic Cycle”, Proc. Nat. Acad. Sci. U.S.A. 2007, 104, 20641-20642.

Liptak, M. D.; Fleischhacker, A. S.; Matthews, R.; Brunold, T. C. “Probing the Role of the Histidine 759 Ligand in Cobalamin-Dependent Methionine Synthase”, Biochemistry 2007, 46, 8024-8035.

Yikilmaz, E.; Porta, J.; Vahedi-Faridi, A.; Grove, L.; Bronshteyn, Y.; Brunold, T. C.; Borgstahl, G. E. O.; Miller, A.-F. “How can a Single Second Sphere Amino Acid Change Cause a Reduction Midpoint   Potential Change of Hundreds of mV?”, J. Am. Chem. Soc. 2007, 129, 9927-9940.

Pierce, B. S.; Gardner, J. D.; Bailey, L. J.; Brunold, T. C.; Fox, B. G. “Characterization of the Nitrosyl Adduct of Substrate-Bound Mouse Cysteine Dioxygenase by Electron Paramagnetic Resonance:  Electronic Structure of the Active Site and Mechanistic Implications”, Biochemistry 2007, 46, 8569-8578.

Bierman, M. J.; Van Heuvelen, K. M.; Schmeisser, D.; Brunold, T. C.; Jin, S. “Ferromagnetic Semiconducting EuO Nanorods”, Adv. Mater. 2007, 19, 2677-2681.

Fiedler, A. T.; Brunold, T. C. “Spectroscopic and Computational Studies of Ni³⁺ Complexes with Mixed S/N Ligation:  Implications for the Active-Site of Ni Superoxide Dismutase”, Inorg. Chem. 2007, 46, 8511-8523.

Kieber-Emmons, M. T.; Annaraj, J.; Seo, M. S.; Van Heuvelen, K. M.; Tosha, T.; Kitagawa, T.; Brunold, T. C.; Nam, W.; Riordan, C. G. “Identification of an “End-on” Nickel-Superoxo Adduct, [Ni(tmc)(O₂)]⁺”, J. Am. Chem. Soc. 2006; 128, 14230-14231.

Liptak, M. D.; Brunold, T. C. “Spectroscopic and Computational Studies of Co¹⁺Cobalamin: Spectral and Electronic Properties of the “Superreduced” B₁₂ Cofactor”, J. Am. Chem. Soc. 2006, 128, 9144-9156.

Dey, M.; Kunz, R. C.; Van Heuvelen, K. M.; Craft, J. L.; Horng, Y.-C.; Tang, Q.; Bocian, D. F.; George, S. J.; Brunold, T. C.; Ragsdale, S. W. “Spectroscopic and Computational Studies of Reduction of the Metal versus the Tetrapyrrole Ring of Coenzyme F₄₃₀ from Methyl-Coenzyme M Reductase”, Biochemistry 2006, 45, 11915-11933.

Fiedler, A. T.; Brunold, T. C. “Spectroscopic and Computational Insights into the Geometric, Electronic, and Magnetic Properties of the H-Cluster of Fe-Only Hydrogenases and Relevant Model Complexes”, Chemtracts-Inorganic Chemistry 2005, 18, 653-666.

Stich, T. A.; Seravalli, J.; Venkateshrao, S.; Spiro, T. G.; Ragsdale, S. W.; Brunold, T. C. “Spectroscopic Studies of the Corrinoid/Iron-Sulfur Protein from Moorella thermoacetica”, J. Am. Chem. Soc. 2006, 128, 5010-5020.

Fiedler, A. T.; Brunold, T. C. “Computational Studies of the H-Cluster of Fe-Only Hydrogenases:  Geometric, Electronic, and Magnetic Properties, and their Dependence on the [Fe₄S₄] Cubane”, Inorg. Chem. 2005, 44, 9322-9344.

Brooks, A. J.; Fox, C. C.; Marsh, N. G.; Vlasie, M.; Banerjee, R.; Brunold, T. C. “Electronic Structure Studies of the Adenosylcobalamin Cofactor in Glutamate Mutase”, Biochemistry 2005, 44, 15167-15181.

Brooks, A. J.; Vlasie, M.; Banerjee, R.; Brunold, T. C. “Co–C Bond Activation in Methylmalonyl-CoA Mutase by Stabilization of the Post-homolysis Product Co²⁺Cobalamin”, J. Am. Chem. Soc. 2005, 127, 16522-16528.

Stich, T. A.; Yamanishi, M.; Banerjee, R.; Brunold, T. C. “Spectroscopic Evidence for the Formation of a Four-Coordinate Co²⁺Cobalamin Species Upon Binding to the Human ATP:Cobalamin Adenosyltransferase”, J. Am. Chem. Soc. 2005, 127, 7660-7661.

Stich, T. A.; Buan, N. R.; Escalante-Semerena, J.; Brunold, T. C. “Spectroscopic and Computational Studies of the ATP:corrinoid Adenosyltransferase (CobA) from Salmonella enterica: Insights into the Mechanism of Adenosylcobalamin Biosynthesis”, J. Am. Chem. Soc. 2005, 127, 8710-8719.

Fiedler, A. T.; Bryngelson, P. A.; Maroney, M. J.; Brunold, T. C. “Spectroscopic and Computational Studies of Ni Superoxide Dismutase: Electronic Structure Contributions to Enzymatic Function”, J. Am. Chem. Soc. 2005, 127, 5449-5462.

Schenker, R.; Mock, M. T.; Kieber-Emmons, M. T.; Riordan, C. G.; Brunold, T. C. “Spectroscopic and Computational Studies on [Ni(tmc)CH₃]OTf: Implications for Ni–Methyl Bonding in the A Cluster of Acetyl-CoA Synthase”, Inorg. Chem. 2005, 44, 3605-3617.

Fiedler, A. T.; Brunold, T. C. “Combined Spectroscopic/Computational Study of Binuclear Fe(I)-Fe(I) Complexes: Implications for the Fully-Reduced Active-Site Cluster of Fe-only Hydrogenases”, Inorg. Chem. 2005, 44, 1794-1809.

Schenker, R.; Kieber-Emmons, M. T.; Riordan, C. G.; Brunold, T. C. “Spectroscopic and Computational Studies on the Trans-m-1,2-Peroxo-Bridged Dinickel(II) Species [{Ni²⁺(tmc)}₂(O₂)](OTf)₂: Nature of End-On Peroxo–Ni(II) Bonding and Comparison with Peroxo–Cu(II) Bonding”, Inorg. Chem. 2005, 44, 1752-1762.

Fiedler, A. T.; Halfen, H. L.; Halfen, J. A.; Brunold, T. C. “Synthesis, Structure Determination, and Spectroscopic/Computational Characterization of a Series of Fe(II)–Thiolate Model Complexes: Implications for Fe–S Bonding in Superoxide Reductases”, J. Am. Chem. Soc. 2005, 127, 1675-1689.

Jackson, T. A.; Karapetian, A.; Miller, A.-F.; Brunold, T. C. “Probing the Geometric and Electronic Structures of the Low-Temperature Azide Adduct and the Product-Inhibited Form of Oxidized Manganese Superoxide Dismutase”, Biochemistry 2005, 44, 1504-1520.

Kieber-Emmons, M. T.; Schenker, R.; Yap, G. P. A.; Brunold, T. C.; Riordan, C. G. “Spectroscopic Elucidation of a Peroxo Ni₂(m-O₂) Intermediate Derived from a Nickel(I) Complex and Dioxygen”, Angew. Chem. 2004, 43, 6716-6718.

Krzystek, J.; Fiedler, A. T.; Sokol, J. J.; Ozarowski, A.; Zvyagin, S. A.; Brunold, T. C.; Long, J. R.; Brunel, L.-C.; Telser, J. “Pseudooctahedral Complexes of Vanadium(III): Electronic Structure Investigation by Magnetic and Electronic Spectroscopy”, Inorg. Chem. 2004, 43, 5645-5658.

Jackson, T. A.; Karapetian, A.; Miller, A.-F.; Brunold, T. C. “Spectroscopic and Computational Studies of the Azide-Adduct of Manganese Superoxide Dismutase: Definitive Assignment of the Ligand Responsible for the Low-Temperature Thermochromism”, J. Am. Chem. Soc. 2004, 126, 12477-12491.

Stich, T. A.; Buan, N. R.; Brunold, T. C. “Spectroscopic and Computational Studies of Co²⁺-Corrinoids: Spectral and Electronic Properties of the Biologically Relevant Base-On and Base-Off Forms of Co²⁺Cobalamin”, J. Am. Chem. Soc. 2004, 126, 9735-9749.

Jackson, T. A.; Brunold, T. C. “Combined Spectroscopic/Computational Studies on Fe- and Mn-dependent Superoxide Dismutases: Insights into Second-Sphere Tuning of Active Site Properties”, Acc. Chem. Res. 2004, 37, 461-470.

Brunold, T. C. “Spectroscopic and Computational Insights into the Geometric and Electronic Properties of the A Cluster of Acetyl-Coenzyme A Synthase”, J. Biol. Inorg. Chem. 2004, 9, 533-541.

Fujita, K.; Schenker, R.; Gu, W.; Brunold, T. C.; Cramer, S. P.; Riordan, C. G. “A Monomeric Nickel–Dioxygen Adduct Derived from O₂ and a Ni(I) Complex”, Inorg. Chem. 2004, 43, 3324-3326.

Brooks, A. J.; Vlasie, M.; Banerjee, R.; Brunold, T. C. “Spectroscopic and Computational Studies on the Adenosylcobalamin-Dependent Methylmalonyl-CoA Mutase: Evaluation of Enzymatic Contributions to Co–C Bond Activation in the Co³⁺ Ground State”, J. Am. Chem. Soc. 2004, 126, 8167-8180.

Fox, D. C.; Fiedler, A. T.; Halfen, H. L.; Brunold, T. C.; Halfen, J. A. “Electronic Structure Control of the Nucleophilicity of Transition Metal-Thiolate Complexes: An Experimental and Theoretical Study”, J. Am. Chem. Soc. 2004, 126, 7627-7638.

Craft, J. L.; Horng, Y.-C.; Radgsdale, S. W.; Brunold, T. C. “Nickel Oxidation States of F₄₃₀ Cofactor in Methyl-Coenzyme M Reductase”, J. Am. Chem. Soc. 2004, 126, 4068-4069.

Brunold, T. C. “Combined Spectroscopic/Computational Studies of Metal Centers in Proteins and Cofactors: Application to Coenzyme B₁₂”, CHIMIA 2004, 58, 186-193.

Krzystek, J.; Zvyagin, S. A.; Ozarowski, A.; Fiedler, A. T.; Brunold, T. C.; Telser, J. “Definitive Spectroscopic Determination of Zero-Field Splitting in High-Spin Cobalt(II)”, J. Am. Chem. Soc. 2004, 126, 2148-2155.

Craft, J. L.; Horng, Y.-C.; Radgsdale, S. W.; Brunold, T. C. “Spectroscopic and Computational Characterization of the Nickel-Containing F₄₃₀ Cofactor of Methyl-Coenzyme M Reductase”, J. Biol. Inorg. Chem. 2004, 9, 77-89.

Schenker, R. P.; Brunold, T. C. “Computational Studies on the A cluster of Acetyl-Coenzyme A Synthase: Geometric and Electronic Properties of the NiFeC Species and Mechanistic Implications”, J. Am. Chem. Soc. 2003, 125, 13962-13963.

Jackson, T. A.; Yikilmaz, E.; Miller, A.-F.; Brunold, T. C. “Spectroscopic and Computational Study of a Non-Heme Iron {Fe-NO}⁷ System: Exploring the Geometric and Electronic Structures of the Nitrosyl Adduct of Iron Superoxide Dismutase”, J. Am. Chem. Soc. 2003, 125, 8348-8363.

Stich, T. A.; Brooks, A. J.; Buan, N. R.; Brunold, T. C. “Spectroscopic and Computational Studies of Co³⁺-Corrinoids: Spectral and Electronic Properties of the B₁₂ Cofactors and Biologically Relevant Precursors”, J. Am. Chem. Soc. 2003, 125, 5897-5914.

Craft, J. L.; Mandimutsira, B. S.; Fujita, K.; Riordan, C. G.; Brunold, T. C. “Spectroscopic Studies of a Ni¹⁺–CO Model Complex: Implications for the CO Dehydrogenase and Acetyl-CoA Synthase Catalytic Mechanisms”, Inorg. Chem. 2003, 43, 859-867.

Maliekal, J.; Karapetian, A.; Vance, C.; Yikilmaz, E.; Wu, Q.; Jackson, T. A.; Brunold, T. C.; Spiro, T. G.; Miller, A.-F. “Comparison and Contrasts between the Active Site pKs of Mn-Superoxide Dismutase and Those of Fe-Superoxide Dismutase”, J. Am. Chem. Soc. 2002, 124, 15064-15075.

Schenker, R.; Mandimutsira, B. S.; Riordan, C. G.; Brunold, T. C. “Spectroscopic and Computational Studies on [(PhTt^tBu)₂Ni₂(m-O)₂]: Nature of the Bis-m-oxo (Ni³⁺)₂ “Diamond” Core”, J. Am. Chem. Soc. 2002, 124, 13842-13855.

Jackson, T. A.; Xie, J.; Yikilmaz, E.; Miller, A.-F.; Brunold, T. C. “Spectroscopic and Computational Studies on Iron and Manganese Superoxide Dismutases: Nature of the Chemical Events Associated with Active Site pKs”, J. Am. Chem. Soc. 2002, 124, 10833-10845.

Xie, J.; Yikilmaz, E.; Miller, A.-F.; Brunold, T. C. “Second-Sphere Contributions to Substrate-Analog Binding in Iron(III) Superoxide Dismutase”, J. Am. Chem. Soc. 2002, 124, 3769-3774.

Yikilmaz, E.; Xie, J.; Brunold, T. C.; Miller, A.-F. “Hydrogen-Bond-Mediated Tuning of the Redox Potential of the Non-Heme Fe Site of Superoxide Dismutase”, J. Am. Chem. Soc. 2002, 124, 3482-3483.

Craft, J. L.; Ludden, P. W.; Brunold, T. C. “Spectroscopic Studies of Nickel-Deficient Carbon Monoxide Dehydrogenase from Rhodospirillum rubrum: Nature of the FeS Clusters”, Biochemistry 2002, 41, 1681-1688.

Mandimutsira, B. S.; Yamarik, J. L.; Brunold, T. C.; Gu, W.; Cramer, S. P.; Riordan, C. G. “Dioxygen Activation by a Nickel Thioether Complex: Characterization of a Ni^III₂(m-O)₂ Core”, J. Am. Chem. Soc. 2001, 123, 9194-9195.