Publications

2021 to present

Tucci, F. J.; Jodts, R. J.; Hoffman, B. M.; Rosenzweig, A. C. Product analogue binding identifies the copper active site of particulate methane monooxygenase. Nat. Catal. 2023, x, x

Manesis, A. C.; Slater, J. W.; Cantave, K.; Bollinger, Jr., J. M.; Krebs, C.; Rosenzweig, A. C. Capturing a bis-Fe(IV) state in Methylosinus trichosporium OB3b MbnH. Biochemistry 2023, 62, 1082

Koo, C. W.; Hershewe, J. M.; Jewett, M. C.; Rosenzweig, A. C. Cell-free protein synthesis of particulate methane monooxygenase into nanodiscs. ACS Synth. Biol. 2022, 11, 4009

Zhu, Y.; Koo, C. W.; Cassidy, C. K.; Spink, M. C.; Ni, T.; Zanetti-Domingues, L. C.; Bateman, B.; Martin-Fernandez, M. L.; Shen, J.; Sheng, Y.; Song, Y.; Yang, Z.; Rosenzweig, A. C.; Zhang, P. Structure and activity of particulate methane monooxygenase arrays in methanotrophs. Nat. Commun. 2022, 13, 5221.

Schachner,L. F.; Des Soye, B.; Ro, S.; Kenney, G. E.; Ives, A. N.; Su, T.; Goo, Y. A.; Jewett, M. C.; Rosenzweig, A. C.; Kelleher, N. L. Revving an engine of human metabolism: activity enhancement of triosephosphate isomerase via hemi-phosphorylation. ACS Chem. Biol. 2022, 17, 2769

Park, Y. J.; Jodts, R. J.; Slater, J. W.; Reyes, R. M.; Winton, V. J.; Montaser, R. A.; Thomas, P. M.; Dowdle, W. B.; Ruiz, A.; Kelleher, N. L.; Bollinger, J. M., Jr.; Krebs, C.; Hoffman, B. M. Rosenzweig, A. C. A mixed valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis. Proc. Natl. Acad. Sci. USA 2022, 119, e2123566119.

Koo, C. W.; Tucci, F. J.; He, Y.; Rosenzweig, A. C. Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer. Science 2022, 375, 1287.

Hadley, R. C.; Zhitnitsky, D.; Livnat-Levanon, N.; Masrati, G.; Vigonsky, E.; Rose, J.; Ben-Tal, N.; Rosenzweig, A. C.; Lewinson, O. The copper-linked Escherichia coli AZY operon: Structure, metal binding, and a possible physiological role in copper delivery. J. Biol. Chem. 2022, 298, 101445.

Park, Y. J.; Roberts, G. M.; Montaser, R.; Kenney, G. E.; Thomas, P. M.; Kelleher, N. L.; Rosenzweig, A. C. Characterization of a copper-chelating natural product from the methanotroph Methylosinus sp. LW3. Biochemistry 2021, 60, 2845.

Jodts, R. J.; Ross, M. O.; Koo, C. W.; Doan, P. E.; Rosenzweig, A. C.; Hoffman, B. M. Coordination of the copper centers in particulate methane monooxygenase: comparison between methanotrophs and characterization of the Cu_C site by EPR and ENDOR spectroscopies. J. Am. Chem. Soc. 2021, 143, 15358.

Manesis, A. C.; Jodts, R. J.; Hoffman, B. M.; Rosenzweig, A. C. Copper binding by a unique family of metalloproteins is dependent on kynurenine formation. Proc. Natl. Acad. Sci. USA 2021, 118, e2100680118.

Cutsail, G. E., III; Ross, M. O.; Rosenzweig, A. C.; DeBeer, S. Toward a unified understanding of the copper sites in particulate methane monooxygenase: an X-ray absorption spectroscopic investigation. Chem. Sci. 2021, 12, 6194.

Koo, C. W.; Rosenzweig, A. C. Biochemistry of aerobic biological methane oxidation. Chem. Soc. Rev. 2021, 50, 3424.

2016 to 2020

Koo, C. W.; Rosenzweig, A. C. Particulate methane monooxygenase and the PmoD protein. In Encyclopedia of Inorganic and Bioinorganic Chemistry 2020, DOI: 10.1002/9781119951438.eibc2740.

Fisher, O. S.; Sendzik, M. R.; Ross, M. O.; Lawton, T. J.; Hoffman, B. M.; Rosenzweig, A. C. PCu_AC domains from methane-oxidizing bacteria use a histidine brace to bind copper. J. Biol. Chem. 2019, 294, 16351.

Kenney, G. E.; Dassama, L. M. K.; Manesis, A. C.; Ross, M. O.; Chen, S.; Hoffman, B. M.; Rosenzweig, A. C. MbnH is a diheme MauG-like protein associated with microbial copper homeostasis. J. Biol. Chem. 2019, 294, 16141.

Ro, S. Y.; Schachner, L. F.; Koo, C. W.; Purohit, R.; Remis, J. P.; Kenney, G. E.; Liauw, B. W.; Thomas P. M.; Patrie, S. M.; Kelleher, N. L.; Rosenzweig, A. C. Native top-down mass spectrometry provides insights into the copper centers of membrane-bound methane monooxygenase. Nat. Commun. 2019, 10, 2675.

Ross, M. O.; MacMillan, F.; Wang, J.; Nisthal, A.; Lawton, T. J.; Olafson, B. D.; Mayo, S. L.; Rosenzweig, A. C.; Hoffman, B. M. Particulate methane monooxygenase contains only monocopper centers. Science 2019, 364, 566-570.

Ross, M. O.; Fisher, O. S.; Morgada, M. N.; Krzyaniak, M. D.; Wasielewski, M. R.; Vila, A. J.; Hoffman, B. M.; Rosenzweig, A. C. Formation and electronic structure of an atypical Cu_A site. J. Am. Chem. Soc. 2019, 141, 4678-4686.

Fisher, O. S.; Kenney, G. E.; Ross, M. O.; Lemma, B. E.; Batelu, S.; Thomas, P. M.; Sosnowski, V. C.; DeHart, C. J.; Kelleher, N. L.; Stemmler, T. L.; Hoffman, B. M.; Rosenzweig, A. C. Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteria. Nat. Commun. 2018, 9, 4276.

Deng, Y. W.; Ro, S. Y.; Rosenzweig, A. C. Structure and function of the lanthanide‐dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C. J. Biol. Inorg. Chem. 2018, 23, 1037-1047.

Ro, S. Y.; Ross, M. O.; Deng, Y. W.; Batelu, S.; Lawton, T. J.; Hurley, J. D.; Stemmler, T. L.; Hoffman, B. M.; Rosenzweig, A. C. From micelles to bicelles: effect of the membrane on particulate methane monooxygenase activity. J. Biol. Chem. 2018, 293, 10457-10465.

Park, Y. J.; Kenney, G. E.; Schachner, L. F.; Kelleher, N. L.; Rosenzweig, A. C. Repurposed HisC aminotransferases complete the biosynthesis of some methanobactins. Biochemistry 2018, 57, 3515-3523.

Kenney, G. E.; Rosenzweig, A. C. Chalkophores. Annu. Rev. Biochem. 2018, 87, 645-676.

Ro, S. Y.; Rosenzweig, A. C. Recent advances in the genetic manipulation of Methylosinus trichosporium OB3b. Methods Enzymol. 2018, 605, 335-349.

Kenney, G. E.; Dassama, L. M. K.; Pandelia, M.-E.; Gizzi, A. S.; Martinie, R. J.; Gao, P.; DeHart, C. J.; Schachner, L. F.; Skinner, O. S.; Ro, S. Y., Zhu, X.; Sadek, M.; Thomas, P. M.; Almo, S. C.; Bollinger, J. M., Jr.; Krebs, C.; Kelleher, N. L.; Rosenzweig, A. C. The biosynthesis of methanobactin. Science 2018, 359, 1411-1416.

Purohit, R.; Ross, M. O.; Batelu, S.; Kusowski, A.; Stemmler, T. L.; Hoffman, B. M.; Rosenzweig, A. C. A Cu+-specific CopB transporter: revising P1B-type ATPase classification. Proc. Natl. Acad. Sci. USA 2018, 115, 2108-2113.

Kenney, G. E.; Rosenzweig, A. C. Methanobactins: maintaining copper homeostasis in methanotrophs and beyond. J. Biol. Chem. 2018, 293, 4606-4615.

Cao, L.; Caldararu, O.; Rosenzweig, A. C.; Ryde, U. Quantum refinement does not support dinuclear copper sites in the crystal structures of particulate methane monooxygenase. Angew. Chem. Int. Ed. 2018, 57, 162-166.

Rosenzweig, A. C. A biochemical sulfur delivery service. Science 2017, 358, 307-308.

Ross, M. O.; Rosenzweig, A. C. A tale of two methane monooxygenases. J. Biol. Inorg. Chem. 2017, 22, 307-319.

Dassama, L. M. K.; Kenney; G. E.; Rosenzweig, A. C. Methanobactin: from genome to function. Metallomics 2017, 9, 7-20.

Dassama, L. M. K.; Kenney; G. E.; Ro, S. Y.; Zielazinski, E. L.; Rosenzweig, A. C. Methanobactin transport machinery. Proc. Natl. Acad. Sci. USA 2016, 113, 13027-13032.

Lawton, T. J.; Rosenzweig, A. C. Biocatalysts for methane conversion: big progress on breaking a small substrate. Curr. Op. Chem. Biol. 2016, 35, 142-149.

Trana, E. N; Nocek, J. M.; Vander Woude, J.; Span, I.; Smith, S. M.; Rosenzweig, A. C.; Hoffman, B. M. Charge-disproportionation symmetry breaking creates a heterodimeric myoglobin complex with enhanced affinity and rapid intracomplex electron transfer. J. Am. Chem. Soc. 2016, 138, 12615-12628.

Kenney, G. E.; Goering, A. W.; Ross, M. O.; DeHart, C. J.; Thomas, P. M.; Hoffman, B. M.; Kelleher, N. L.; Rosenzweig, A. C. Characterization of methanobactin from Methylosinus sp. LW4. J. Am. Chem. Soc. 2016, 138, 11124-11127.

Lawton, T. J.; Rosenzweig, A. C. Methane-oxidizing enzymes: an upstream problem in biological gas-to-liquids conversion. J. Am. Chem. Soc. 2016, 138, 9327-9340.

Blanchette, C. D.; Knipe, J. M.; Stolaroff, J. K.; DeOtte, J. R.; Oakdale, J. S.; Maiti, A.; Lenhardt, J. M.; Sirajuddin, S.; Rosenzweig, A. C.; Baker, S. E. Printable enzyme-embedded materials for methane to methanol conversion. Nat. Commun. 2016, 7, 11900.

Lawton, T. J.; Rosenzweig, A. C. Methane – make it or break it. Science 2016, 352, 892-893.

Kenney, G. E.; Sadek, M.; Rosenzweig, A. C. Copper-responsive gene expression in the methanotroph Methylosinus trichosporium OB3b. Metallomics 2016, 8, 931-940.

Lawton, T. J.; Kenney, G. E.; Hurley, J. D.; Rosenzweig, A. C. The CopC family: structural and bioinformatic insights into a diverse group of periplasmic copper binding proteins. Biochemistry 2016, 55, 2278-2290.

Kathman, S. G.; Span, I.; Smith, A. T.; Xu, Z.; Zhan, J.; Rosenzweig, A. C.; Statsyuk, A. V. A small molecule that switches a ubiquitin ligase from a processive to a distributive enzymatic mechanism. J. Am. Chem. Soc. 2015, 137, 12442-12445.

Li, J.; Lawton, T. J.; Kostecki, J. S.; Nisthal, A.; Fang, J.; Mayo, S. L.; Rosenzweig, A. C.; Jewett, M. C. Cell-free protein synthesis enables high yielding synthesis of an active multicopper oxidase. Biotechnol. J. 2016, 11, 212-218.

2011 to 2015

Smith, A. T.; Barupala, D.; Stemmler, T. L.; Rosenzweig, A. C. A new metal binding domain involved in cadmium, cobalt, and zinc transport. Nat. Chem. Biol. 2015, 11, 678-684.

Sirajuddin, S.; Rosenzweig, A. C. Enzymatic oxidation of methane. Biochemistry 2015, 54, 2283-2294.

Rosenzweig, A. C. Breaking methane. Nature 2015, 518, 309-310.

Culpepper, M. A.; Rosenzweig, A. C. Structure and protein-protein interactions of methanol dehydrogenase from Methylococcus capsulatus (Bath). Biochemistry 2014, 53, 6211-6219.

Sirajuddin, S.; Rosenzweig, A. C. Protocols for structural and functional analysis of particulate methane monooxygenase from Methylocystis species strain Rockwell (ATCC 49242). Hydrocarbon and Lipid Microbiology Protocols 2014 (T. J. McGenity et al, eds.), Berlin: Springer-Verlag,10.1007/8623_2014_22.

Sirajuddin, S.; Barupala, D.; Helling, S.; Marcus, K.; Stemmler, T. L.; Rosenzweig, A. C. Effects of zinc on particulate methane monooxygenase activity and structure. J. Biol. Chem. 2014 289, 21782-21794.

Culpepper, M. A.; Cutsail, G. E., III; Gunderson, W. A.; Hoffman, B. M.; Rosenzweig, A. C. Identification of the valence and coordination environment of the particulate methane monooxygenase copper centers by advanced EPR characterization. J. Am. Chem. Soc. 2014, 136, 11767-11775.

Chang, W.; Guo, Y.; Wang, C.; Butch, S. E.; Rosenzweig, A. C.; Boal, A. K.; Krebs, C.; Bollinger, J. M., Jr. Mechanism of the C5 Stereoinversion Reaction in the Biosynthesis of Carbapenem Antibiotics. Science 2014, 343, 1140-1144.

Silakov, A.; Grove, T. L.; Radle, M. I.; Bauerle, M. R.; Green, M. T.; Rosenzweig, A. C.; Boal, A. K.; Booker, S. J. Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. J. Am. Chem. Soc. 2014, 136, 8221-8228.

Smith, A. T.; Smith, K. P.; Rosenzweig, A. C. Diversity of the metal-transporting P1B-type ATPases. J. Biol. Inorg. Chem. 2014, 6, 947-960.

Austin, R. N.; Kenney, G. E.; Rosenzweig, A. C. Perspective: what is known, and not known, about the connections between alkane oxidation and metal uptake in alkanotrophs in the marine environment. Metallomics 2014, 6, 1121-1125.

Lawton, T. J.; Ham, J.; Sun, T.; Rosenzweig, A. C. Structural conservation of the B subunit in the ammonia monooxygenase/particulate methane monooxygenase superfamily. Proteins: Struct., Funct., Bioinf. 2014, 82, 2263-2267.

Makhlynets, O.; Boal, A.K.; Rhodes, D.V.; Kitten, T.; Rosenzweig, A.C.; Stubbe, J. Streptococcus sanguinis class Ib ribonucleotide reductase: high activity with both iron and manganese cofactors and structural insights. J. Biol. Chem. 2014, 289, 6259-72.

Zielazinski, E. L.; González-Guerrero, M.; Subramanian, P.; Stemmler, T. L.; Argüello, J. M.; Rosenzweig, A. C. Sinorhizobium meliloti Nia is a P_1B-5-ATPase expressed in the nodule during plant symbiosis and is involved in Ni and Fe transport. Metallomics 2013, 5, 1614-1623.

Dassama, L. M. K.; Krebs, C.; Bollinger, J. M., Jr.; Rosenzweig, A. C.; Boal, A. K. Structural Basis for Assembly of the Mn^IV/Fe^III Cofactor in the Class Ic Ribonucleotide Reductase from Chlamydia trachomatis. Biochemistry. 2013 52, 6424−6436.

Lawton, T. J.; Bowen, K. E.; Sayavedra-Soto, L.A.; Arp, D. J.; Rosenzweig, A.C. Characterization of a Nitrite Reductase Involved in Nitrifier Denitrification. J. Biol. Chem. 2013, 288, 25575–25583.

Rosenzweig, A. C. Metalloenzymes: Put a ring on it. Nature Chem. Biol. 2013, 9, 220-221.

Kenney, G. E. and Rosenzweig, A. C. Genome mining for methanobactins. BMC Biol. 2013, 11, 17.

Zielazinski, E. L.; Cutsail, G. E., III; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. Characterization of a cobalt-specific P_1B-ATPase. Biochemistry 2012, 51, 7891-7900.

Boal, A. K. and Rosenzweig, A.C. A Radical Route for Nitrogenase Carbide Insertion. Science 2012, 337, 1617-1618.

Culpepper, M. A. and Rosenzweig, A. C. Architecture and active site of particulate methane monooxygenase. Crit. Rev. Biochem. Mol. Biol. 2012, 47, 483-492.

Culpepper, M. A.; Cutsail, G. E., III; Hoffman, B. M.; Rosenzweig, A. C. Evidence for oxygen binding at the active site of particulate methane monooxygenase. J. Am. Chem. Soc. 2012, 134, 7640-7643.

Boal, A. K.; Cotruvo, J. A., Jr.; Stubbe, J.; Rosenzweig, A. C. The dimanganese(II) site of Bacillus subtilis class Ib ribonucleotide reductase. Biochemistry 2012, 51, 3861-3871.

Dassama, L. M. K.; Boal, A. K.; Krebs, C.; Rosenzweig, A. C.; Bollinger, J. M., Jr. Evidence that the β subunit of Chlamydia trachomatis ribonucleotide reductase is active with the manganese ion of its manganese(IV)/iron(III) cofactor in site 1. J. Am. Chem. Soc. 2012, 134, 2520-2523.

Kenney, G. E.; Rosenzweig, A. C. Chemistry and biology of the copper chelator methanobactin. ACS Chem. Biol. 2011, 7, 260-268.

Smith, S. M.; Rawat, S.; Telser, J.; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M. Biochemistry 2011, 50, 10231-10240.

Balasubramanian, R.; Kenney, G. E.; Rosenzweig, A. C. Dual pathways for copper uptake by methanotrophic bacteria. J. Biol. Chem. 2011, 286, 37313-37319.

Smith, S. M.; Rosenzweig, A. C. Particulate methane monooxygenase. In Encyclopedia of Metalloproteins (V.N. Uversky, R.H. Kretsinger, E.A. Permyakov, eds.), 2012, Springer, Heidelberg, Germany, in press.

Lawton, T. J.; Rosenzweig, A. C. Detection and characterization of a multicopper oxidase from Nitrosomonas europaea. Methods Enzymol. 2011, 496, 423-433.

Boal, A. K.; Grove, T. L.; McLaughlin, M. I.; Yennawar, N. H.; Booker, S. J.; Rosenzweig, A. C. Structural basis for methyl transfer by a radical SAM enzyme. Science 2011, 332, 1089-1092.

Rosenzweig, A. C. Particulate methane monooxygenase. In Handbook of Metalloproteins Volumes 4 and 5 (A. Messerschmidt, ed.), 2011, John Wiley & Sons, Chichester, UK, 615-622, originally published online September 2008.

Lawton, T. J.; Rosenzweig, A. C. Two-domain multicopper oxidase. In Handbook of Metalloproteins Volumes 4 and 5 (A. Messerschmidt, ed.), 2011, John Wiley & Sons, Chichester, UK, 591-599, originally published online September 2010.

Smith, S. M.; Balasubramanian, R.; Rosenzweig, A. C. Metal reconstitution of particulate methane monooxygenase and heterologous expression of the pmoB subunit. Methods Enzymol. 2011, 495, 195-210.

Benítez, J. J.; Keller, A. M.; Huffman, D. L.; Yatsunyk, L. A.; Rosenzweig, A. C.; Chen, P. Relating dynamic protein interactions of metallochaperones with metal transfer at the single-molecule level. Faraday Dis. 2011, 148, 71-82.

2006 to 2010

Balasubramanian, R.; Levinson, B. T.; Rosenzweig, A. C. Secretion of flavins by three species of methanotrophic bacteria. Appl. Environ. Microbiol. 2010, 76, 7356-7358.

Boal, A. K.; Cotruvo, J. A., Jr.; Stubbe, J.; Rosenzweig, A. C. Structural basis for activation of class Ib ribonucleotide reductase. Science 2010, 329, 1526-1530.

Traverso, M. E.; Subramanian, P.; Davydov, R.; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. Identification of a hemerythrin-like domain in a P1B-type transport ATPase. Biochemistry 2010, 49, 7060-7068.

Balasubramanian, R.; Smith, S. M.; Rawat, S.; Yatsunyk, L. A.; Stemmler, T. L.; Rosenzweig, A. C. Oxidation of methane by a biological dicopper center. Nature 2010, 465, 115-119.

Walker, C. B.; de la Torre, J. R.; Urakawa, H.; Klotz, M. G.; Lawton, T. J.; Pinel, N.; Arp, D. J.; Brochier-Armanet, C.; Chain, P. S. G.; Chan, P. P.; Golabgir, A.; Hemp, J.; Hügler, M.; Karr, E. A.; Könneke, M.; Shin, M.; Lawton, T. J.; Martens-Habbena, W.; Sayavedra-Soto, L. A.; Lang, D.; Sievert, S. M.; Rosenzweig, A. C.; Manning, G.; Stahl, D. A. The Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea. Proc. Natl. Acad. Sci. USA 2010, 107, 8818-8823.

Agarwal, S.; Hong, D.; Desai, N. K.; Sazinsky, M. H., Argüello, J. M.; Rosenzweig, A. C. Structure and interactions of the C-terminal metal binding domain of Archaeoglobus fulgidus CopA. Proteins 2010, 78, 2450-2458.

Ukaegbu, U. E.; Kantz, A.; Beaton, M.; Gassner, G. T.; Rosenzweig, A. C. Structure and ligand binding properties of the epoxidase component of styrene monooxygenase. Biochemistry 2010, 49, 1678-1688.

Rosenzweig, A. C. Zeroing in on a new copper site. Nature Chem. 2009, 1, 684-685.

Barker, K. D.; Eckermann, A. L.; Sazinsky, M. H.; Hartings, M. R.; Abajian, C.; Georganopoulou, D. G.; Ratner, M. A.; Rosenzweig, A. C.; Meade, T. J. Protein binding and the electronic properties of iron(II) complexes: an electrochemical and optical investigation of outer sphere effects. Bioconjugate Chem. 2009, 20, 1930-1939.

Boal, A. K.; Rosenzweig, A. C. Crystal structures of cisplatin bound to a human copper chaperone. J. Am. Chem. Soc. 2009, 131, 14196-14197.

Boal, A. K.; Rosenzweig, A. C. Structural biology of copper trafficking. Chem. Rev. 2009, 109, 4760-4779.

Lawton, T. J.; Sayavedra-Soto, L. A.; Arp, D. J.; Rosenzweig, A. C. Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins. J. Biol. Chem. 2009, 284, 10174-10180.

Ukaegbu, U. E.; Rosenzweig, A. C. Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS. Biochemistry 2009, 48, 2207-2215

Rosenzweig, A. C. The metal centers of particulate methane monooxygenase. Biochem. Soc. Trans. 2008, 36, 1134-1137.

Banci, L.; Bertini, I.; Cantini, F.; Rosenzweig, A. C.; Yatsunyk, L. A. Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1. Biochemistry 2008, 47, 7423-7429.

Hakemian, A. S.; Kondapalli, K. C.; Telser, J.; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry 2008, 47, 6793-6801.

Balasubramanian, R. ; Rosenzweig, A. C. Copper methanobactin: a molecule whose time has come. Curr. Op. Chem. Biol. 2008, 12, 245-249.

Benítez, J. J.; Keller, A. M.; Huffman, D. L.; Yatsunyk, L. A.; Rosenzweig, A. C.; Chen, P. Probing transient copper-chaperone-Wilson disease protein interactions at the single-molecule level with nanovesicle trapping. J. Am. Chem. Soc. 2008, 130, 2446-2447.

Yatsunyk, L. A., Easton, J. A., Kim, L. R., Sugarbaker, S. A., Bennett, B., Breece, R. M., Vorontsov, I. I., Tierney, D. L., Crowder, M. W., & Rosenzweig, A. C. Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli. J. Biol. Inorg. Chem. 2008, 13, 271-288.

Sazinsky, M. H., LeMoine, B., Orofino, M., Davydov, R., Bencze, K. Z., Stemmler, T. L., Hoffman, B. M., Argüello, J. M., & Rosenzweig, A. C. Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus. J. Biol. Chem. 2007, 282, 25950-25959.

Balasubramanian, R. ; Rosenzweig, A. C. Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase. Acc. Chem. Res. 2007, 40, 573-580.

Hakemian, A. S.; Rosenzweig, A. C. The biochemistry of methane oxidation. Ann. Rev. Biochem. 2007, 76, 223-241.

Wheeler, K. E.; Nocek, J. M.; Cull, D. A.; Yatsunyk, L. A.; Rosenzweig, A. C.; Hoffman, B. M. Dynamic docking of cytochrome b5 with myoglobin and a-hemoglobin: heme-neutralization ‘squares’ and the binding of electron-transfer-reactive configurations. J. Am. Chem. Soc. 2007, 129, 3906-3917.

Yatsunyk, L. A.; Rosenzweig, A. C. Copper binding and transfer by the N-terminus of the Wilson disease protein. J. Biol. Chem. 2007, 282, 8622-8631.

Sommerhalter, M.; Zhang, Y.; Rosenzweig, A. C. Solution structure of the COMMD1 N-terminal domain. J. Mol. Biol. 2007, 365, 715-721.

Rosenzweig, A. C.; Sazinsky, M. H. Structural insights into dioxygen-activating copper enzymes. Curr. Op. Struct. Biol. 2006, 16, 729-735.

Lieberman, R. L.; Kondapalli, K. C.; Shrestha, D. B.; Hakemian, A. S.; Smith, S. M.; Telser, J.; Kuzelka, J.; Gupta, R.; Borovik, A. S.; Lippard, S. J.; Hoffman, B. M.; Rosenzweig, A. C.; Stemmler, T. L. Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy. Inorg. Chem. 2006, 45, 8372-8381.

Ukaegbu, U. E.; Henery, S.; Rosenzweig, A. C. Biochemical characterization of MmoS, a sensor protein involved in copper-dependent regulation of soluble methane monooxygenase. Biochemistry 2006, 45, 10191-10198.

Sazinsky, M. H.; Agarwal, S.; Argüello, J. M.; Rosenzweig, A. C. Structure of the actuator domain from the Archaeglobus fulgidus Cu1+-ATPase. Biochemistry 2006, 45, 9949-9955.

Abajian, C.; Rosenzweig, A. C. Crystal structure of yeast Sco1. J. Biol. Inorg. Chem. 2006, 11, 459-456.

Sazinsky, M. H.; Mandal, A. L; Argüello, J. M.; Rosenzweig, A. C. Structure of the ATP binding domain from the Archaeglobus fulgidus Cu1+-ATPase. J. Biol. Chem. 2006, 281, 11161-11166.

2001 to 2005

Hakemian, A. S.; Tinberg, C. E.; Kondapalli, K. C.; Telser, J.; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. The copper chelator methanobactin from Methylosinus trichosporium OB3b binds Cu(I). J. Am. Chem. Soc., 2005, 127, 17142-17143.

Sommerhalter, M.; Saleh, L.; Bollinger, J. M., Jr.; Rosenzweig , A. C. Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122. Acta cryst. 2005, D61, 1649-1654.

Lieberman, R. L.; Rosenzweig, A. C. The quest for the particulate methane monooxygenase active site. Dalton Trans. 2005, 21, 3390-3396.

Lieberman, R. L.; Rosenzweig, A. C. Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane, Nature 2005, 434, 177-182.

Sommerhalter, M.; Lieberman, R. L.; Rosenzweig, A. C. X-ray crystallography and biological metal centers: is seeing believing?, Inorg. Chem. 2005, 44, 770-778.

Abajian, C.; Yatsunyk, L. A.; Ramirez, B. E.; Rosenzweig, A. C. Solution structure and binding of copper(I) by yeast Cox17. J. Biol. Chem. 2004, 279, 53584-53592.

Lieberman, R. L.; Rosenzweig, A. C. Crystallographic trapping of a precatalytic enzyme complex provides new insight into dioxygen activation at a mononuclear copper center. Chemtracts 2004, 17, 562-568.

Sommerhalter, M.; Voegtli, W. C.; Perlstein, D. L.; Ge, J.; Stubbe, J.; Rosenzweig, A. C. Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers. Biochemistry 2004, 43, 7736-7742.

Lieberman, R. L. ; Rosenzweig, A. C. Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase. Crit. Rev. Biochem. Mol. Biol. 2004, 39, 147-164.

Wernimont, A. K.; Yatsunyk, L. A.; Rosenzweig, A. C. Binding of copper(I) by the Wilson disease protein and its copper chaperone. J. Biol. Chem. 2004, 269, 12269-12276.

Voegtli, W. C.; Sommerhalter, M.; Saleh, L.; Baldwin, J.; Bollinger, J. M., Jr.; Rosenzweig, A. C. Variable coordination geometries at the diiron(II) active site of ribonucleotide reductase R2. J. Am. Chem. Soc. 2003, 125, 15822-15830.

Miller, M. T.; Gerratana, B.; Stapon, A.; Townsend, C. A.; Rosenzweig, A. C. Crystal structure of carbapenam synthetase (CarA). J. Biol. Chem. 2003, 278, 40996-41002.

Lieberman, R. L.; Shrestha, D. B.; Doan, P. F.; Hoffman, B. M.; Stemmler, T. L.; Rosenzweig, A. C. Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster. Proc. Natl. Acad. Sci. USA 2003, 100, 3820-3825.

Lieberman, R. L.; Rosenzweig, A. C. Metal ion homeostasis. In Comprehensive Coordination Chemistry II: From Biology to Nanotechnology (J. McCleverty, T. J. Meyer, eds.), 2003, Oxford:Pergamon, pp. 195-211.

Wernimont, A. K.; Huffman, D. L.; Finney, L. A.; Demeler, B.; O’Halloran, T.V.; Rosenzweig, A. C. Crystal structure and dimerization equilibria of PcoC, a methionine-rich copper resistance protein from Escherichia coli. J. Biol. Inorg. Chem. 2003, 8, 185-194.

Miller, M. T.; Bachmann, B. O.; Townsend, C. A.; Rosenzweig, A. C. The catalytic cycle of b-lactam synthetase observed by x-ray crystallographic snapshots. Proc. Natl. Acad. Sci. USA 2002, 99, 14752-14757.

Rosenzweig, A. C. Metallochaperones: bind and deliver. Chem. Biol. 2002, 9, 673-677.

Lamb, A. L.; Torres, A. S.; O’Halloran, T. V.; Rosenzweig, A. C. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nature Struct. Biol. 2001, 8, 751-755.

Voegtli, W. C.; Ge, J.; Perlstein, D. L.; Stubbe, J.; Rosenzweig, A. C. Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer. Proc. Natl. Acad. Sci. USA 2001, 98, 10073-10078.

Miller, M. T.; Bachmann, B. O.; Townsend, C. A.; Rosenzweig, A. C. Structure of b-lactam synthetase reveals how to synthesize antibiotics instead of asparagine. Nature Struct. Biol. 2001, 8, 684-689.

Baldwin, J.; Voegtli, W. C.; Khidekel, N.; Moënne-Loccoz, P.; Krebs, C.; Pereira, A. S.; Ley, B. A.; Huynh, B. H.; Loehr, T. M.; Riggs-Gelasco, P. J.; Rosenzweig, A. C.; Bollinger, J. M., Jr. Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase. J. Am. Chem. Soc. 2001, 123, 7017-7030.

Lieberman, R. L.; Arciero, D. M.; Hooper, A. B.; Rosenzweig, A. C. Crystal structure of a novel red copper protein from Nitrosomonas europaea. Biochemistry 2001, 40, 5674-5681.

Rosenzweig, A. C. Copper delivery by metallochaperone proteins. Acc. Chem. Res. 2001, 34, 119-128.

Whittington, D. A.; Rosenzweig, A. C.; Frederick, C. A.; Lippard, S. J. Xenon and halogenated alkanes track putative substrate binding cavities in the soluble methane monooxygenase hydroxylase. Biochemistry 2001, 40, 3476-3482.

1996 to 2000

Voegtli, W. C.; Reiter, N. J.; White, D. J.; Rusnak, F.; Rosenzweig, A. C. Structure of the bacteriophage l Ser/Thr protein phosphatase with sulfate ion bound in two coordination modes. Biochemistry 2000, 39, 15365-15374.

Wernimont, A. K.; Huffman, D. L.; Lamb, A. L.; O’Halloran, T. V.; Rosenzweig, A. C. Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nature Struct. Biol. 2000, 7, 766-771.

Lamb, A. L; Torres, A. S.; O’Halloran, T. V.; Rosenzweig, A. C. Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry 2000, 39, 14720-14727.

Voegtli, W. C.; Khidekel, N.; Baldwin, J.; Ley, B. A.; Bollinger, J. M.; Jr.; Rosenzweig, A. C. Crystal structure of the ribonucleotide reductase R2 mutant that accumulates a m-1,2-peroxodiiron(III) intermediate during oxygen activation. J. Am. Chem. Soc. 2000, 122, 3255-3261.

Rosenzweig, A. C. Nitrous oxide reductase from CuA to CuZ. Nature Struct. Biol. 2000, 7, 169-171.

Rosenzweig, A. C.; O’Halloran, T. V. Structure and chemistry of the copper chaperone proteins. Curr. Op. Chem. Biol. 2000, 4, 140-147.

Lamb, A. L.; Wernimont, A. K.; Pufahl, R. A.; O’Halloran, T. V.; Rosenzweig, A. C. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry 2000, 39, 1589-1595.

Coufal, D. E.; Blazyk, J. L.; Whittington, D. A.; Wu, W. W.; Rosenzweig, A. C.; Lippard, S. J. Sequencing and analysis of the Methylococcus capsulatus (Bath) soluble methane mono-oxygenase genes. Eur. J. Biochemistry 2000, 267, 2174-2185.

Lamb, A. L.; Wernimont, A. K.; Pufahl, R. A.; Culotta, V. C.; O’Halloran, T. V.; Rosenzweig, A. C. Crystal structure of the copper chaperone for superoxide dismutase. Nature Struct. Biol. 1999, 6, 724-729.

Portnoy, M. E.; Rosenzweig, A. C.; Rae, T.; Huffman, D. L.; O’Halloran, T. V.; Culotta, V. C. Structure-function analyses of the Atx1 metallochaperone. J. Biol. Chem. 1999, 274, 15041-15045.

Rosenzweig, A. C.; Huffman, D. L.; Hou, M. Y.; Wernimont, A. K.; Pufahl, R. A.; O’Halloran, T. V. Crystal structure of the Atx1 metallochaperone protein at 1.02 Å resolution. Structure 1999, 7, 605-617.

Rosenzweig, A. C.; Brandstetter, H.; Whittington, D. A.; Nordlund, P.; Lippard, S. J.; Frederick, C. A. Crystal structure of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. Proteins 1997, 29, 141-152.

Rosenzweig, A. C.; Lippard, S. J. Structure and biochemistry of methane monooxygenase enzyme systems. In Iron and Related Transition Metals in Microbial Metabolism (G. Winkelmann, C. J. Carrano, eds.), 1997, Reading: Harwood Academic Publishers, pp. 257-279.

Rosenzweig, A. C.; Frederick, C. A.; Lippard, S. J. Carboxylate shifts in the active site of the hydroxylase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath). In Microbial Growth on C1 Compounds: Proceedings of the Eighth International Symposium, (M. E. Lidstrom, F. R. Tabita, eds.), 1996, Dordrecht: Kluwer Academic Publishers, pp. 141-149.

Dooley, D. M.; Alvarez, M. L; Rosenzweig, A. C.; Hollis, R. S.; Zumft, W. G. Exogenous ligand binding to Pseudomonas stutzeri nitrous oxide reductase. Inorg. Chim. Acta 1996, 242, 239-244.