Majhi, S; Roy, P; Jo, M; Liu, J; Hurto, R; Freddolino, L; Marsh, ENG (2025) Viperin expression leads to downregulation of mitochondrial genes through misincorporation of ddhCTP by mitochondrial RNA polymerase. J. Biol. Chem 301(4) 108359 DOI10.1016/j.jbc.2025.108359
Datar, PM; Roy, P; Mondal, A; Marsh, ENG (2024) Characterization of the N5-dimethylallyl-FMN Intermediate in the Biosynthesis of Prenylated-FMN Catalyzed by UbiX. BIOCHEMISTRY DOI10.1021/acs.biochem.4c00410
DiRocco, DJ ; Roy, P ; Mondal, A ; Datar, PM ; Marsh, ENG. (2024) An Enzyme Catalyzing the Oxidative Maturation of Reduced Prenylated-FMN to Form the Active Coenzyme ACS CATALYSIS 14 (13): 10223-10233. DOI10.1021/acscatal.4c02747
Mondal, A ; Roy, P ; Carrannatto, J; Datar, PM ; Dirocco, DJ ; Hunter, K; Marsh, ENG. (2024) Surveying the scope of aromatic decarboxylations catalyzed by prenylated-flavin dependent enzymes FARADAY DISCUSSIONS. 252 (0): 208-222. DOI10.1039/d4fd00006d
Datar, PM.; Joshi, SY; Deshmukh, SA; Marsh, ENG. (2024) Probing the role of protein conformational changes in the mechanism of prenylated-FMN-dependent phenazine-1-carboxylic acid decarboxylase J. Biol. Chem. 301(4) 108359. DOI10.1016/j.jbc.2025.108359
A. K. Kaneshiro, P. M. Datar, E. N. G. Marsh (2023). "Negative Cooperativity in the Mechanism of Prenylated-Flavin-Dependent Ferulic Acid Decarboxylase: A Proposal for a "Two-Stroke" Decarboxylation Cycle" Biochem. 62 (1): 53-61. DOI: 10.1021/acs.biochem.2c00460
A. Patel, K. Koebke, T. Grunkemeyer, C. Riordan, Y. Kim, R. Bailey, E. N. G. Marsh (2022). "Purification of the full-length, membrane-associated form of the antiviral enzyme viperin utilizing nanodiscs" Sci. Reps. 12(1). DOI: 10.1038/s41598-022-16233-z
TY. Lu, W. Guo, P.M. Datar, Y. Xin, E. N. G. Marsh, Z. Chen (2022). "Probing protein aggregation at buried interfaces: distinguishing between adsorbed protein monomers, dimers, and a monomer-dimer mixture in situ" Chem. Sci. 13(4): 975-984.
S. Ghosh, E.N.G. Marsh (2022). "Viperin-taken down with a pinch of salt." EMBO Reps. 23(1). DOI: 10.15252/embr.202154258
H. Chia, K. Koebke, A. Rangajaran, N. Koropatkin, ENG. Marsh, J. Biteen (2021). "New Orange Ligand-Dependent Fluorescent Reporter for Anaerobic Imaging" ACS Chem. Biol. 16(11): 2109-2115
P. M. Datar, E. N. G. Marsh (2021). "Decarboxylation of Aromatic Carboxylic Acids by the Prenylated-FMN-dependent Enzyme Phenazine-1-carboxylic Acid Decarboxylase" ACS Catal. 11(18): 11723-11732
A. Patel, E. N. G. Marsh (2021). "The Antiviral Enzyme, Viperin, Activates Protein Ubiquitination by the E3 Ubiquitin Ligase, TRAF6." J. Am. Chem. Soc. 143(13): 4910-4914
A.K. Kaneshiro, K.J. Koebke, C. Zhao, K.L. Ferguson, D.P. Ballou, B.A. Palfey, B.T. Ruotolo, E.N.G. Marsh (2021). "Kinetic Analysis of Transient Intermediates in the Mechanism of Prenyl-Flavin-Dependent Ferulic Acid Decarboxylase." Biochemistry 60(2): 125-134.
T. Chazovachii, M. Somers, M. Robo, D. Collias, M. James, ENG. Marsh, P. Zimmerman, J. Alfaro, A. McNeil (2021). "Giving superabsorbent polymers a second life as pressure-sensitive adhesives." Nat. Comm. 12(1). DOI: 10.1038/s41467-021-24488-9
W. Guo, X. Zou, H. Jiang, K. Koebke, M. Hoarau, R. Crisci, TY. Lu, T. Wei, ENG. Marsh, Z. Chen (2021). "Molecular Structure of the Surface-Immobilized Super Uranyl Binding Protein" J. Phys. Chem. B 125(28):7706-7716. DOI: 10.1021/acs.jpcb.1c03849
N.A. Miller, A.K. Kaneshiro, A. Konar, R. Alonso-Mori, A. Britz, A. Deb, J.M. Glownia, J.D. Koralek, L. Mallik, J.H. Meadows, L.B. Michocki, T.B. van Driel, M. Koutmos, S. Padmanabhan, M. Elias-Arnanz, K.J. Kubarych, E.N.G. Marsh, J.E. Penner-Hahn, R.J. Sension (2020). "The Photoactive Excited State of the B12-Based Photoreceptor CarH." J. Phys. Chem. B. 124(47): 10732-10738.
L. Liu, A.B. Dumbrepatil, A.S. Feischhacker, E.N.G. Marsh, S.W. Ragsdale (2020). "Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site." J. Biol. Chem. 295(50): 17227-17240.
S. Ghosh and E.N.G. Marsh (2020). "Viperin: An ancient radical SAM enzyme finds its place in modern cellular metabolism and innate immunity." J. Biol. Chem. 295(33): 11513-11528.
H.E. Chia, T. Zuo, N.M. Koropatkin, E.N.G. Marsh, J.S. Biteen (2020). "Imaging living obligate anaerobic bacteria with bilin-binding fluorescent proteins." Curr. Res. Micro. Sci. 1: 1-6.
A.B. Dumbrepatil, K.A. Zegalia, K. Sajja, R.T. Kennedy, E.N.G. Marsh (2020). "Targeting viperin to the mitochondrion inhibits the thiolase activity of the trifunctional enzyme complex." J. Biol. Chem. 295(9): 2839-2949.
S. Ghosh, A.M. Patel, T.J. Grunkemeyer, A.B. Dumbrepatil, K. Zegalia, R.T. Kennedy, E.N.G. Marsh (2020). "Interactions between Viperin, Vesicle-Associated Membrane Protein A, and Hepatitis C Virus Protein NS5A Modulate Viperin Activity and NS5A Degradation." Biochemistry 59(6): 780-789.
M. Hoarau, K.J. Koebke, Z. Chen, E.N.G. Marsh (2019). "Probing Metal Ion Discrimination in a Protein Designed to Bind Uranyl Cation with Femtomolar Affinity." Front. Mol. Biosci. 6:73.
A.S. Cristie-David, E.N.G. Marsh (2019). "Metal-Dependent Assembly of a Protein Nano-Cage." Protein Sci. 28(9): 1620-1629.
A.S. Cristie-David, J. Chen, D.B. Nowak, A.L. Bondy, K. Sun, S. Park, M.M. Banaszak-Holl, M. Su, E.N.G. Marsh (2019). "Coiled-Coil-Mediated Assembly of an Icosahedral Protein Cage with Extremely High Thermal and Chemical Stability." J. Am. Chem. Soc. 141(23):9207-9216.
H.E. Chia, E.N.G. Marsh, J.S. Biteen (2019). "Extending fluorescence microscopy into anaerobic environments." Curr. Opin. Chem. Biol. 51:98-104.
M. Xiao, S. Wei, J. Chen, C.L. Brooks, E.N.G. Marsh, Z. Chen (2019). "Molecular Mechanisms of Interactions between Monolayered Transition Metal Dichalogenides and Biological Molecules." J. Am. Chem. Soc. 141(25):9980-9988.
A.B. Dumbrepatil, S. Ghosh, K.A. Zegalia, P.A. Malec, J.D. Hoff, R.T. Kennedy, E.N.G. Marsh (2019). "Viperin interacts with the kinase IRAK1 and the E3 ubiquitin ligase TRAF6, coupling innate immune signaling to antiviral ribonucleotide synthesis." J. Biol. Chem. 294(17): 6888-6898.
X. Zou, S. Wei, S. Badieyan, M. Schroeder, J. Jasensky, C.L. Brooks, E.N.G. Marsh (2018). "Investigating the Effect of Two-Point Surface Attachment on Enzyme Stability and Activity." J. Am. Chem. Soc. 140(48):16560-16569.
A.S. Cristie-David, P. Koldewey, B.A. Meinen, J.C.A. Bardwell, E.N.G. Marsh (2018). "Elaborating a coiled coil-assembled octahedral protein cage with additional protein domains." Protein Science. 27(11):1893-1900.
J. Jasnesky, K. Ferguson, M. Baria, X. Zou, R. McGinnis, A. Kaneshiro, S. Badieyan, S. Wei, E.N.G. Marsh, Z. Chen (2018). "Simultaneous Observation of the Orientation and Activity of Surface-Immobilized Enzymes." Langmuir. 34(31): 9133-9140.
Y. Li, T.L. Ogorzalek, S. Wei, X. Zhang, P. Yang, J. Jasensky, C.L. Brooks, E.N.G. Marsh, Z. Chen (2018). "Effect of immobilization site on the orientation and activity of surface-tethered enzymes." Phys. Chem. Chem. Phys. 3;20(2): 1021-1029
N. Arunrattanamook and E.N.G. Marsh (2018). "Kinetic Characterization of Prenyl-flavin Synthase from Saccharomyces cerevisiae." Biochemistry. 6;57(5): 696-700
M. Hoarau, S. Badieyan, E.N.G. Marsh (2017). "Immobilized enzymes: understanding enzyme - surface interactions at the molecular level." Org. Biomol. Chem. 15, 9539-9551
S. Badieyan, A. Sciore, J.D. Eschweiler, P. Koldewey, A.S. Cristie-David, B.T. Ruotolo, J.C.A. Bardwell, M. Su, E.N.G. Marsh (2017). "Symmetry-Directed Self-Assembly of a Tetrahedral Protein Cage Mediated by de Novo-Designed Coiled Coils." ChemBio Chem. 18, 1888-1892
K.L. Ferguson, J.D. Eschweiler, B.T. Ruotolo, E.N.G. Marsh (2017). "Evidence for a 1,3-Dipolar Cyclo-addition Mechanism in the Decarboxylation of Phenylacrylic Acids Catalyzed by Ferulic Acid Decarboxylase." J. Am. Chem. Soc. 139, 10972-10975
R.L. Merzel, C. Frey, J. Chen, R. Garn, M. van Dongen, C.A. Dougherty, A.K. Kandaluru, P.S. Low, E.N.G Marsh, M.M. Banaszak Holl (2017). "Conjugation Dependent Interaction of Folic Acid with Folate Binding Protein." Bioconjug. Chem. 28, 2350-2360
M.M. Schroeder, Q. Wang, S. Badieyan, Z. Chen, E.N.G. Marsh (2017). "Effect of Surface Crowding and Surface Hydrophilicity on the Activity, Stability and Molecular Orientation of a Covalently Tethered Enzyme." Langmuir. 33, 7152-7159
S. Badieyan, Q. Wang, X. Zou, Y. Li, M. Herron, N.L. Abbott, Z. Chen and E.N.G. Marsh (2017). “An Engineered Surface-immobilized Enzyme that Retains High Levels of Catalytic Activity in Air.” J. Am. Chem. Soc. 139, 2872 – 2875
R.L. Merzel, S.M. Boutom, J. Chen, C. Frey, K. Shedden, E.N.G. Marsh and M.M. Banaszak Holl (2017). “Folate binding protein: therapeutic natural nanotechnology for folic acid, methotrexate, and leucovorin.” Nanoscale 9, 2603 – 2615
A. Sciore and E.N.G. Marsh (2017). “Symmetry-Directed Design Protein Cages and Protein Lattices and their Applications.” Subcellular Biochemistry 83, 195 – 224
A.S. Cristie-David, A. Sciore, S. Badieyan, J.D. Eschweiler, P. Koldewey, B.T. Ruotolo, J.C.A. Bardwell, and E.N.G. Marsh (2017). “Evaluation of de novo-designed coiled-coils as off-the-shelf components for protein assembly.” Molec. Syst. Design Engin. DOI 10.1039/C7ME00012J
E.N.G. Marsh (2016). "Designing fluorinated proteins." Methods Enzymol. 580, 251 – 278
A. Sciore, M. Su, P. Koldewey, J.D. Eschweiler, K.A. Diffley, B.M. Linhares, B.T. Ruotolo, J.C.A. Bardwell, G. Skiniotis and E.N.G. Marsh (2016). “A flexible, symmetry-directed approach to assembling protein cages.” Proc. Natl. Acad. Sci. USA 113, 8681 – 8686
C. Makins, S. Ghosh, G.D. Román-Meléndez, P.A. Malec, R.T. Kennedy and E.N.G. Marsh (2016). “Does Viperin Function as a Radical S-adenosyl-L-methionine-dependent Enzyme in Regulating Farnesylpyrophosphate Synthase Expression and Activity?” J. Biol. Chem. 291, 26806 – 26815
K.L. Ferguson, N. Arunrattanamook, and E.N.G. Marsh (2016). “Mechanism of the novel prenylated flavin-containing enzyme ferulic acid decarboxylase probed by isotope effects and linear free energy relationships.” Biochemistry 55, 2857–2863
B.R. Ellington, B. Paul, D. Das, A.K. Vitek, P.M. Zimmerman and E.N.G. Marsh (2016). “An unusual iron-dependent oxidative deformylation reaction providing insight into hydrocarbon biosynthesis in Nature.” ACS Catal., 6, 3293–3300
E.N.G. Marsh (2016). “Whither enzymology in the twenty first century?” Front. Chem. 4: doi: 10.3389/fchem.2016.00020
S.W. Sun, B.C. Buer, E.N.G. Marsh and R.T. Kennedy (2016). “A label-free Sirtuin 1 assay based on droplet electrospray ionization mass spectrometry.” Anal. Meth., 8, 3458-3465
J. Chen, M.A. van Dongen, R.L. Merzel, C.A. Dougherty, B.G. Orr, A.K. Kanduluru, P.S. Low, E.N.G. Marsh, and M.M. Banaszak Holl (2016). “Substrate-triggered exosite binding: Synergistic dendrimer/folic acid action for achieving a specific, tight-binding to folate binding protein.” Biomacromolecules, 17, 922–927
L. Shen, K.C.K. Cheng, M. Schroeder, P. Yang, F-G. Wu, E. N. G. Marsh, J. Lahann and Z. Chen (2016). “Immobilization of Enzymes on Polymer Surfaces.” Surface Science, 648, 53-59
M.A. Fink, E.N.G. Marsh and C.L. Drennan (2015). "Substrate-bound Structures of Benzylsuccinate Synthase Reveal how Toluene is Activated in Anaerobic Hydrocarbon Degradation.” J. Biol. Chem., 290, 22398 - 22408
S. Kotler, J.R. Brender, S. Vivekanandan, Y. Suzuki, K. Yamamoto, M. Monette, J. Krishnamoorthy, M.M. Banaszak Holl, E.N.G. Marsh and A. Ramamoorthy (2015). “High-Resolution NMR Characterization of Low Abundance Oligomers of Amyloid-β Without Purification.” Scientific Reports, 5:11811 | DOI: 10.1038/srep11811
T.L. Ogorzalek, S. Wei, Y. Liu, C.L. Brooks III, Z. Chen, and E.N.G. Marsh (2015). “Molecular-Level Insights into Orientation-Dependent Changes in the Thermal Stability of Enzymes Covalently Immobilized on Surfaces.” Langmuir, 31, 6145–6153
R.L. Merzel, J. Chen, E.N.G. Marsh, and M.M. Banaszak Holl (2015). “Folate Binding Protein – Outlook for Drug Delivery Applications.” Chin. Chem. Lett, 26, 426 - 430
F. Lin, X.N. Lin and E.N.G. Marsh (2015). “Recent Progress in Hydrocarbon Biofuel Biosynthesis: Pathways and Enzymes.” Chin. Chem. Lett, 26, 431 - 434
Y. Li, S. Wei, J. Wu, J. Jasensky, C. Xi, H. Li, Y. Xu, Q. Wang, E.N.G. Marsh, C.L. Brooks, Z. Chen (2015). "Effects of Peptide Immobilization Sites on the Structure and Activity of Surface-Tethered Antimicrobial Peptides." J. Phys. Chem. C., 119, 7146 - 7155
F. Lin, K.L. Ferguson, D.R. Boyer, X.N. Lin and E.N.G. Marsh (2015). “Isofunctional Enzymes PAD1 and UbiX Catalyze Formation of a Novel Cofactor Required by Ferulic Acid Decarboxylase and 4-Hydroxy-3-polyprenylbenzoic Acid Decarboxylase.” ACS Chem. Biol., 10, 1137 - 1144
B.C. Buer, B. Paul, D. Das, J.A. Stuckey and E.N.G. Marsh (2014). “Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Bound.” ACS Chem. Biol., 9, 2584 - 2593
E.N.G. Marsh (2014). “Fluorinated proteins: from design and synthesis to structure and stability.” Acc Chem. Res., 47, 2878 - 2886
J. Wang, R.P. Woldring, G.D. Román-Meléndez, A.M. McClain, B.R. Alzua and E.N.G. Marsh (2014). “Recent advances in radical SAM enzymology: new structures and mechanisms.” ACS Chem. Biol., 9, 1929 - 1938
M.W. Waugh and E. N. G. Marsh (2014). “Solvent Isotope Effects on Alkane Formation by Cyanobacterial Aldehyde Deformylating Oxygenase and Their Mechanistic Implications.” Biochemistry, 53, 5537 - 5543
M.A. Fink, E.T. Judd, S.J. Elliot, E.N.G. Marsh and C.L. Drennan (2014). “Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity.” Proc. Natl. Acad. Sci., 111, 10161 - 10166
D. Das, B. Paul, B. Ellington and E.N.G. Marsh (2014). “Mechanistic insights from reaction of a-oxiranyl-aldehydes with cyanobacterial aldehyde deformylating oxygenate.” ACS Chem. Biol., 9, 570 - 577
G. D. Román-Meléndez, P. von Glehn, J. N. Harvey, A. J. Mulholland, and E. N. G. Marsh (2014). "Role of Active Site Residues in Promoting Cobalt-Carbon Bond Homolysis in Adenosylcobalamin-Dependent Mutases Revealed through Experimentation and Computation." Biochemistry 53, 169-177
Y. Suzuki and E.N.G. Marsh (2014). “Using 19F NMR to Probe Biological Interactions of Proteins and Peptides.” ACS Chem. Biol., 9 1242–1250
M. Goel, E. N. G. Marsh, Z. Chen and N. L. Abbott (2014). “Comparison of the Influence of Humidity and D-Mannitol on the Organization of Tetra (Ethylene Glycol)-Terminated Self-Assembled Monolayers and Immobilized Antimicrobial Peptides.” Langmuir, 30 7143–7151
L. Shen, M. Schroeder, T. L. Ogorzalek, P. Yang, F-G. Wu, E. N. G. Marsh and Z. Chen (2014). “Surface Orientation Control of Site-Specifically Immobilized Nitro-reductase (NsfB).” Langmuir, 30 5930–593
D.P. Patterson, M. Su, T.M. Franzmann, A. Sciore, G. Skiniotis and E.N.G. Marsh (2014). “Characterization of a highly flexible self-assembling protein system designed to form nano cages.” Protein Science 23, 190 - 199
M.W. Waugh and E. N. G. Marsh (2013). “Aldehyde decarbonylases: Enigmatic enzymes of hydrocarbon biosynthesis”. ACS Catalysis, 3, 2515 - 2521
Y. Liu, T. L. Ogorzalek, P. Yang, E. N. G. Marsh and Z. Chen (2013). “Molecular orientation of enzymes attached to surfaces through defined chemical linkages at the solid/liquid interface”. J. Am. Chem. Soc., 135, 12660 - 12669
B. Khara, N. Menon, C. Levy, D. Mansell, D. Das, E. N. G. Marsh, D. Leys and N. S. Scrutton (2013). "Production of propane and other short chain alkanes by structure-based engineering of ligand specificity in aldehyde deformylating oxygenate". ChemBioChem, 14, 1204 -1208
F. Lin, N. X. Lin. and E.N.G. Marsh (2013). “Aldehyde-forming fatty acyl-CoA reductase from cyanobacteria: expression, purification and characterization of the recombinant Enzyme”. FEBS J., 280, 4773-478
B.C. Buer, B.L. Levin and E.N.G. Marsh (2013). “Design of fluorous proteins”. Methods Molec. Biol.
Y. Suzuki, J.R. Brender, M. Soper, J. Krishnamoorthy, Y. Zhou, N. Kotov, B. Ruotolo, A. Ramamoorthy and E.N.G. Marsh (2013). “Resolution of oligomeric species during the aggregation of Aβ1-40 using 19F NMR". Biochemistry, 52, 1903 -1912
B.C. Buer, B.L. Levin and E.N.G. Marsh (2013). “Perfluoro-tert-butyl-homoserine as a sensitive 19F NMR reporter for peptide-membrane interactions in solution”. J. Peptide Sci., 19, 308 - 314
B.C. Buer, J.L. Meagher, J.A. Stuckey and E.N.G. Marsh (2012). "Comparison of the structures and stabilities of coiled-coil proteins containing hexafluoroleucine and t-butylalanine provides insight into the stabilizing effects of highly fluorinated amino acid side-chains". Protein Science, 21 1705 - 1715
B.C. Buer, J.L. Meagher, J.A. Stuckey and E.N.G. Marsh (2012). “Structural Basis for the Enhanced Stability of Highly Fluorinated Proteins”. Proc. Natl. Acad. Sci. USA, 109, 4810 - 4815
B.C. Buer and E.N.G. Marsh (2012). “Fluorine: a new element in protein design”. Protein Science, 21 453 - 462
E.N.G Marsh and G.D. Román Meléndez (2012). “Adenosylcobalamin enzymes: theory and experiment begin to converge”. Biochem. Biophys. Acta, 1824, 1154 – 1164
B.C. Buer, B.L. Levin and E.N.G. Marsh (2012). “Influence of Fluorination on the Thermodynamics of Protein Folding”. J. Am. Chem. Soc, 134, 13027 - 13034
B.E. Eser, D. Das, J. Han, P.R. Jones and E.N.G. Marsh (2011). “Oxygen-Independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: investigation of kinetics and requirement for an external electron donor”. Biochemistry, 50, 10743–10750
D.P. Patterson, A.M. Desai, M.M. Banaszak Holl and E.N.G. Marsh (2011). “Evaluation of a symmetry-based strategy for assembling protein complexes”. RSC Advances, 1 1004 -1012
Y. Suzuki, B.C. Buer, H.M. Al Hashimi and E.N.G. Marsh (2011). “Using Fluorine NMR to Probe Changes in Structure and Dynamics of Membrane-Active Peptides Interacting with the Lipid Bilayer”. Biochemistry, 50, 5979–5987
D. Das, B.E. Eser, J. Han, A. Sciore, and E.N.G. Marsh (2011). "Oxygen-independent decarbonylation of aldehydes by cyano-bacterial aldehyde decarbonylase: a new reaction of di-iron enzymes". Angew. Chem., 50 7148 -7152
B.C. Buer, J. Chugg, H.M. Al Hashimi and E.N.G. Marsh (2010). “Using Fluorine NMR to Probe the Interaction of Membrane-Active Peptides with the Lipid Bilayer”. Biochemistry, 49, 5760 – 5765
M. Kim, E.N.G. Marsh, S-U Kim and J. Han (2010). “Studies on the Conversion of (3S,4R)-Tetrahydrodaidzein to (3S)-Equol by THD Reductase: Proposal for a Mechanism Involving a Radical Intermediate”. Biochemistry, 49, 5582 – 5587
J.R. Brender, K. Hartman, R.P.R. Nanga, N. Popovych, R. de la Salud-Bea, E.N.G. Marsh and A. Ramamoorthy (2010). “Role of Zinc in Human Islet Amyloid Polypeptide Aggregation”. J. Am. Chem. Soc., 132, 8963 – 8973
M.Yoon, H. Song, K. Hakansson and E.N.G. Marsh (2010). “Intrinsic Deuterium Kinetic Isotope Effects in Glutamate Mutase Measured by an Intramolecular Competition Experiment”. Biochemistry. 49, 3168 - 3173
E.N.G. Marsh, D.P. Patterson, and L. Li (2010). “Adenosyl radical: reagent and catalyst in enzyme reactions”. ChemBioChem., 11, 604 -621
B.C. Buer, R. de la Salud-Bea, H.M. Al Hashimi and E.N.G. Marsh (2009). “Engineering protein stability and specificity using fluorous amino acids: the importance of packing effects”. Biochemistry, 48, 10810 - 10817
E.N.G. Marsh, B.C. Buer and A. Ramamoorthy (2009). “Fluorine – a new element in the design of membrane-active peptides”. Molecular Biosystems, 5, 1143 - 1147
E.N.G. Marsh (2009). “Insights into the mechanisms of adenosylcobalamin (coenzyme B12) dependent enzymes from rapid chemical quench experiments”. Biochem. Soc. Trans., 37, 336 - 342
L. Lei, D.P. Patterson, C.C. Fox, B. Lin, P.W. Coschigano and E.N.G. Marsh (2009). “Subunit Structure of Benzylsuccinate Synthase”. Biochemistry 48, 1284–1292
L.M. Gottler, R. de la Salud-Bea, C.E. Shelburne, A. Ramamoorthy and E.N.G. Marsh (2008). “Using Fluorous Amino Acids to Probe the Effects of Changing Hydrophobicity on the Physical and Biological Properties of the α-Hairpin Antimicrobial Peptide Protegrin-1”. Biochemistry. 47, 9243–9250
L.M. Gottler, R. de la Salud-Bea, and E.N.G. Marsh (2008). “The Fluorous Effect in Proteins: Properties of α4F6, a 4-α-Helix Bundle Protein with a Fluorocarbon Core”. Biochemistry. 47, 4484-4490
L.M. Gottler, H-Y Lee, C.E. Shelburne, A. Ramamoorthy and E.N.G. Marsh (2008). “Modulating the biological activity of an antimicrobial peptide using fluorous amino acids”. ChemBioChem. 9, 370-373
H-Y Lee, J.W. Kampf and E.N.G. Marsh (2008). “Covalent metal-peptide framework compounds that extend in one and two dimensions”. Crystal Growth and Design. 8, 296-303
M.Yoon, A. Kalli, H.-Y. Lee, K. Hakansson and E.N.G. Marsh (2007). “Intrinsic Deuterium Kinetic Isotope Effects in Glutamate Mutase Measured by an Intramolecular Competition Experiment”. Angew. Chem. 46, 8455 - 8459
H-Y Lee, M. Yoon and E.N.G. Marsh (2007). “Synthesis of mono- and di-deuterated (2S,3S)-3-methylaspartic acids to facilitate measurement of intrinsic kinetic isotope effects in enzymes”. Tetrahedron, 63, 4663-4668
A. Patwardhan and E.N.G. Marsh (2007). “Changes in the Free Energy Profile of Glutamate Mutase Imparted by the Mutation of an Active Site Arginine Residue to Lysine”. Arch. Biochem. Biophys., 461 194-199
M-C. Cheng and E.N.G. Marsh (2007). “Evidence for Coupled Motion and Hydrogen Tunneling the Reaction Catalyzed by Glutamate Mutase”. Biochemistry, 46, 883-888
G. M. Sandala, D. M. Smith, E. N. G. Marsh and L. Radom (2007). “Towards an Improved Understanding of the Glutamate Mutase System”. J. Am. Chem. Soc., 129 1623-1633
L. Li and E.N.G. Marsh (2006). “Mechanism of Benzylsuccinate Synthase Probed by Substrate Exchange”. J. Am. Chem. Soc., 128, 16056 -16057
L. Li and E.N.G. Marsh (2006). “Deuterium isotope effects in the unusual addition of toluene to fumarate catalyzed by benzylsuccinate synthase”. Biochemistry, 45, 13932 - 13938
M. Yoon, A. Patwardhan, C. Qiao, S. Mansoorabadi, A.L. Menefee, G.R. Reed and E.N.G. Marsh (2006). “The reaction of adenosylcobalamin-dependent glutamate mutase with 2-thioglutarate”. Biochemistry, 45, 11650 - 11657
H.-Y. Lee, K.-H. Lee, H. M. Al Hashimi and E.N.G. Marsh (2006). “Modulating protein structure with fluorous amino acids: increased stability and native-like structure conferred on a 4-helix bundle protein by hexafluoroleucine”. J. Am. Chem. Soc., 128, 337-343
K-H. Lee, C. Cabello, L. Hemmingsen, E.N.G. Marsh and V.L. Pecoraro (2006). “Using nonnatural amino acids to control metal-coordination number in three-stranded coiled coils”. Angew. Chem. Int. Edn., 45 2864 - 2868
J. T. Anderson, P. L. Toogood and E.N.G. Marsh (2005). “Process for preparing single enantiomers of L-5,5,5,5’,5’,5’-hexafluoroleucine and it protected analogs ”. United States Patent, 6974879 B2
A.J. Brooks, C.C. Fox, E.N.G. Marsh, M. Vlasie, R. Banerjee and T. C. Brunold (2005). “Electronic structure studies of the adenosylcobalamin cofactor in glutamate mutase”. Biochemistry, 44, 15167-15181
R.J. Sension, A.D. Harris, A. Stickrath, A.G. Cole, C.C. Fox, and E.N.G. Marsh (2005). “Time-resolved measurements of the photolysis and recombination of adenosylcobalamin bound to glutamate mutase”. J. Phys. Chem. B, 109, 18146-18152
C. Qiao and E.N.G. Marsh (2005). “Mechanism of benzylsuccinate synthase: stereochemistry of toluene addition to fumarate and maleate”. J. Am. Chem. Soc., 127, 8608-8609
M.-C. Cheng and E.N.G. Marsh (2005). “Isotope effects for the transfer of deuterium between glutamate and 5’-deoxyadensosine in adenosylcobalamin-dependent glutamate mutase ”. Biochemistry, 44, 2686-2691
J. T. Anderson, P. L. Toogood and E.N.G. Marsh (2004). “Process for preparing single enantiomers of L-5,5,5,5’,5’,5’-hexafluoroleucine and it protected analogs ”. United States Patent, 6787664 B2
K.-H. Lee, H.-Y. Lee, M.S. Slutsky, J.T. Anderson and E.N.G. Marsh (2004). “Fluorous effect in proteins: De novo design and characterization of a four-alpha-helix bundle protein containing hexafluoroleucine”. Biochemistry, 43, 16277-16284
E.N.G. Marsh, A. Patwardhan and M.S. Huhta (2004). “S-adenosylmethionine radical enzymes”. Bioorganic Chem, 32, 326-340
K.-H. Lee, M. Matzapetakis, S. Mitra, E.N.G. Marsh and V.L. Pecoraro (2004). “Control of metal coordination number through subtle sequence modifications of designed peptides”. J. Am. Chem. Soc., 126, 9178-9179
M.S. Slutsky and E.N.G. Marsh (2004). “Contribution of cation-pi interactions to protein folding studied in a model coiled-coil peptide”. Protein Science, 13, 2244-2251
L Xia, D.P. Ballou and E.N.G. Marsh (2004). “The role of Arg100 in the active site of adenosylcobalamin-dependent glutamate mutase". Biochemistry, 43 3238-3245
R.J. Sension, A.G. Cole, A.D. Harris, C.C. Fox, N. Woodbury, S. Lin, and E.N.G. Marsh (2004). “Photolysis and recombination of adenosylcobalamin bound to glutamate mutase”. J. Am. Chem. Soc, 126, 1598-1599
M.-C. Cheng and E.N.G. Marsh (2004). “Pre-steady state measurement of intrinsic secondary tritium isotope effects associated with the homolysis of adenosylcobalamin and the formation of 5’-deoxyadensosine in glutamate mutase”. Biochemistry, 43, 2155-2158
G. Sciara, S.G. Kendrew, A.E. Miele, E.N.G. Marsh, L. Federici, F. Malatesta, G. Schimperna, C. Savino and B. Vallone (2003). “The structure of ActVA-Orf6: a novel type of monooxygenase involved in actinorhodin biosynthesis”. EMBO J. 22, 205-215
E.N.G. Marsh and W.F. DeGrado (2002). “Non-covalent self assembly of a heterotetrameric diiron protein”. Proc. Natl. Acad. Sci. 99, 5150-5154
M. S. Huhta, D. Ciceri, B.T. Golding and E.N.G. Marsh (2002). “A novel reaction between adenosylcobalamin and 2-methyleneglutarate catalyzed by glutamate mutase”. Biochemistry 41, 3200-3206
H-W. Chih, I. Roymoulik, M. S. Huhta, P. Madhavapeddi and E.N.G. Marsh (2002). “Adenosylcobalamin-dependent glutamate mutase: pre-steady-state kinetic methods for investigating the reaction mechanism”. Methods. Enzymol., 354, 380-399
P. Madhavapeddi, D.P. Ballou and E.N.G. Marsh (2002). “Pre-Steady State Kinetic studies on the Gly171Gln Active Site Mutant of Adenosylcobalamin-dependent Glutamate Mutase”. Biochemistry, 41, 15802-15809
J. T. Anderson, P. L. Toogood and E.N.G. Marsh (2002). “A short and efficient synthesis of L-5,5,5,5’,5’,5’-hexafluoroleucine from N-Cbz-L-serine ”. Org. Lett. 4, 4281-4283
H.-W. Chih and E.N.G. Marsh (2001). “Tritium partitioning and isotope effects in adenosylcobalamin-dependent glutamate mutase”. Biochemistry, 40, 13060-13067
P. Madhavapeddi and E.N.G. Marsh (2001). “The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase”. Chem. Biol, 8, 1143-1149
M. S. Huhta, H.-P. Chen, C. Hemann, C.R. Hille and E.N.G. Marsh (2001). “Protein-Coenzyme interactions in adenosylcobalamin-dependent glutamate mutase”. Biochem. J., 355, 131-137
M. Tollinger, R. Konrat, C. Eichmuller, M.S. Huhta, E.N.G. Marsh and B. Krautler (2001). “The B12-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B12”. J. Mol. Biol., 309, 777-791
B. Hoffman, M. Tollinger, R. Konrat, M. Huhta, E.N.G. Marsh and B. Krautler (2001). “A protein pre-organized to trap the nucleotide moiety of B12: refined solution structure of the B12-binding subunit of glutamate mutase from Clostridium tetanomorphum”. ChemBioChem, 2, 643-655
E.N.G. Marsh and C. L. Drennan (2001). “Adenosylcobalamin-dependent isomerases: new insights into structure and mechanism”. Curr. Opin. Chem. Biol., 5, 499-505
H.-W. Chih and E.N.G. Marsh (2000). “Identification and kinetic competence of glycyl radical as an intermediate in the reaction catalyzed by adenosylcobalamin-dependent glutamate mutase”. J. Am. Chem. Soc, 122, 10732-10733.
I. Roymoulik, N. Moon, W.R. Dunham, D.P. Ballou and E.N.G. Marsh (2000). “Rearrangement of L-2-hydroxyglutarate to L-threo-3-methylmalate catalyzed by adenosylcobalamin-dependent glutamate mutase”. Biochemistry, 39, 10340-10346
E.N.G. Marsh (2000). “Glutamate mutase”. Bioorganic Chemistry, 28, 176-189
E.N.G. Marsh (2000). “Towards the non-stick egg: designing fluorous proteins”. Chemistry and Biology, 7, R153-R157
E.N.G. Marsh and D.E. Holloway (2000). “Adenosylcobalamin-dependent enzymes”. Subcellular Biochemistry, 35, 351-403
S.G. Kendrew, L. Federici, C. Savino, A. Miele, E.N.G. Marsh and B. Vallone (2000). “Crystallization and preliminary x-ray diffraction studies of a monooxygenase from Streptomyces coelicolor A3(2) involved in the biosynthesis of the polyketide actinorhodin”. Acta. Crystalographica, 56, 481-483
E.N.G. Marsh (1999). “Cobalamin dependent enzymes”. Essays in Biochemistry, 34, 139-154
H.-W. Chih and E.N.G. Marsh (1999). “Pre-steady state kinetic investigation of intermediates in the reaction catalyzed by adenosylcobalamin-dependent glutamate mutase”. Biochemistry, 38, 13684-13691
I. Roymoulik, H.-P. Chen and E.N.G. Marsh (1999). “The reaction of the substrate analog 2-ketoglutarate with adenosylcobalamin-dependent glutamate mutase”. J. Biol. Chem. 274, 11619-11622
E.N.G. Marsh and D.P. Ballou (1998). “Coupling of cobalt-carbon bond homolysis and hydrogen atom abstraction in adenosylcobalamin-dependent glutamate mutase”. Biochemistry, 37, 11864-11872
M. Tollinger, R. Konrat, B.H. Hilbert, E.N.G. Marsh and B. Kräutler (1998). “How a protein prepares for B12-binding: structure and dynamics of the B12-binding subunit of glutamate mutase”. Structure, 6 1021-1033
H.-P. Chen and E.N.G. Marsh (1997). “Adenosylcobalamin-dependent glutamate mutase: characterization of an engineered enzyme with simplified quaternary structure and kinetics”. Biochemistry 36 14939-14945
H.-P. Chen and E.N.G. Marsh (1997). “How enzymes control the reactivity of adenosylcobalamin: effect on coenzyme-binding and catalysis of mutations in the conserved histidine-aspartate pair of glutamate mutase”. Biochemistry 36, 7884-7889
S.G. Kendrew, D.A. Hopwood and E.N.G. Marsh (1997). "Physical and mechanistic characterization of the novel mono-oxygenase encoded by the actVA-orf6 gene of Streptomyces coelicolor". J. Bacteriol 179, 4305-4310
E.N.G. Marsh, D.E. Holloway and H.-P. Chen (1997). “Glutamate mutase”. Chapter 16 in Vitamin B12 and B12-Proteins, (B. Kräutler, D. Arigoni and B.T. Golding Eds). Wiley-VCH, Berlin.
D.E. Holloway, H.-P. Chen and E.N.G. Marsh (1996). "Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase — examination of the role of this residue in coenzyme-binding and catalysis". J. Biol Chem., 271, 29121-29125
D.E. Holloway, S.E. Harding and E.N.G. Marsh (1996). "Adenosylcobalamin-dependent glutamate mutase: properties fusion protein in which the cobalamin-binding subunit is linked to the catalytic subunit". Biochem. J., 320, 825-830
E.N.G. Marsh (1995). "Tritium isotope effects in adenosylcobalamin-dependent glutamate mutase: Implications for the Mechanism". Biochemistry, 34, 7542-7547
E.N.G. Marsh (1995). "A radical approach to enzyme catalysis". Bioessays 17, 431-441
S.G. Kendrew, Harding, S.E., D.A. Hopwood and E.N.G. Marsh (1995). "The actVB gene from the actinorhodin biosynthetic cluster encodes a FMN:NADH oxidoredutase: expression, purification and characterization of the recombinant enzyme". J. Biol Chem, 270, 17339-17342
D.E. Holloway and E.N.G. Marsh (1994). "Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum: over-expression in E.coli, purification and characterization of the recombinant enzyme". J. Biol. Chem. 269, 20425-20430
D.E. Holloway and E.N.G. Marsh (1993). "Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum". FEBS Lett. 317, 44-48
E.N.G. Marsh and S.E. Harding (1993). "Methymalonyl-CoA mutase from Propionibacterium shermanii: characterization of the cobalamin inhibited form and subunit-cofactor interactions studied by analytical ultracentrifugation". Biochem. J. 290, 551-555
E.N.G. Marsh and D.E. Holloway (1992). "Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorphum: homologies with other cobalamin-dependent enzymes". FEBS Lett. 310, 147-149