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Johnson, B. J., Yukl, E. T., Klema, V. J., Klinman, J. P., Wilmot, C. M. (2013) Structural snapshots from the oxidative half-reaction of a copper amine oxidase: implications for O2 activation. J. Biol. Chem. 288 (39), 28409-17.
Tarboush, N. A., Yukl, E. T., Shin, S., Feng, M., Wilmot, C. M., Davidson, V. L., (2013) Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG. Biochemistry 52 (37), 6358-67.
Yukl, E. T., Jensen L. M., Davidson, V. L., Wilmot, C. M. (2013) Structures of MauG in complex with quinol and quinone MADH. Acta. Cryst. F. 69, 738-43.
Yukl, E. T., Liu, F., Krzystek, J., Shin, S., Jensen, L. M. R., Davidson, V. L., Wilmot, C. M., Liu, A. (2013) A di-radical intermediate within the context of tryptophan tryptophylquinone biosynthesis. Proc. Natl. Acad. Sci. U. S. A.110 (12), 4569-73.
Wilmot, C. M., Yukl, E. T. (2013) MauG: A di-heme enzyme required for methylamine dehydrogenase maturation. Dalton Trans. 42 (9), 3127-35.
Yukl, E. T., Wilmot, C. M. (2012) Cofactor biosynthesis through protein post-translational modification. Curr. Opin. Chem. Biol. 16 (1-2), 54-9.
Feng, M., Jensen, L. M., Yukl, E. T., Wei, X., Liu, A., Wilmot, C. M., Davidson, V. L. (2012) Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG. Biochemistry 51 (8), 1598-606.
Tarboush, N. A., Jensen, L. M., Yukl, E. T., Geng, J., Liu, A., Wilmot, C. M., Davidson, V. L. (2011) Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 108 (41), 16956-61.
Yukl, E. T., Goblirsch, B. R., Davidson, V. L., Wilmot, C. M. (2011) Crystal structures of the CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: Implications for the mechanism of dioxygen activation. Biochemistry 50 (14), 2931-8.
Yukl, E. T., Ioanoviciu, A., Sivaramakrishnan, S., Nakano, M. M., Ortiz de Montellano, P. R., Moënne-Loccoz, P. (2011) Nitric oxide dioxygenation reaction in DevS and the initial response to nitric oxide in Mycobacterium tuberculosis. Biochemistry 50 (6), 1023-8.
Kommineni, S., Yukl, E. T., Hayashi, T., Delepine, J., Geng, H., Moënne-Loccoz, P., Nakano, M. M. (2010) Nitric oxide-sensitive and –insensitive interaction of Bacillus subtillis NsrR with a ResDE-controlled promoter. Mol. Microbiol. 78 (5), 1280-93.
Yukl, E. T., Jepkorir, G., Alontaga, A. Y., Pautsch, L., Rodriguez, J. C., Rivera, M., Moënne-Loccoz, P. (2010) Kinetic and spectroscopic studies of hemin acquisition in the hemophore HasAp from Pseudomonas aeruginosa. Biochemistry 49 (31), 6646-54.
Jepkorir, G., Rodriguez, J. C., Rui, H., Im, W., Lovell, S., Battaile, K. P., Alontaga, A. Y., Yukl, E. T., Moënne-Loccoz, P., Rivera, M. (2010) Structural, NMR spectroscopic, and computational investigation of hemin loading in the hemophore HasAp from Pseudomonas aeruginosa. J. Am. Chem. Soc. 132 (28), 9857-72.
Yukl, E. T., de Vries, S., Moënne-Loccoz, P. (2009) The millisecond intermediate in the reaction of nitric oxide with oxymyoglobin is an iron(III)-nitrato complex, not a peroxynitrite. J. Am. Chem. Soc. 131 (21), 7234-35.
Alontaga, A. Y., Rodrigurez, J. C., Shönbrunn, E., Becker, A., Funke, R., Yukl, E. T., Hayashi, T., Stobaugh, J., Moënne-Loccoz, P., Rivera, M. (2009) Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein−protein interactions between holo-HasAp and hemoglobin. Biochemistry 48 (1) 96-109.
Yukl, E. T., Elbaz, M. A., Nakano, M. M., Moënne-Loccoz, P. (2008) Transcription factor NsrR from Bacillus subtilis senses nitric oxide with a 4Fe−4S cluster. Biochemistry 47 (49), 13084-13092.
Yukl, E. T., Ioanoviciu, A., Nakano, M. M., Ortiz de Montellano, P. R., Moënne-Loccoz, P. (2008). A distal tyrosine residue is required for ligand discrimination in DevS from Mycobacterium tuberculosis. Biochemistry 47 (47), 12532-9.
Yukl, E. T., Ioanoviciu, A., de Montellano. P. R., Moënne-Loccoz, P. (2007). Interdomain interactions within the two-component heme-based sensor DevS from Mycobacterium tuberculosis. Biochemistry 46 (34), 9728-36.
Ioanoviciu, A., Yukl, E. T., Moënne-Loccoz, P., de Montellano P. R. (2007). DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis. Biochemistry 46 (14), 4250-60.
Whittaker, M. M., Pan, H. Y., Yukl E. T., Whittaker, J. W. (2007). Burst kinetics and redox transformations of the active site manganese ion in oxalate oxidase: Implications for the catalytic mechanism. J. Biol. Chem. 282 (10), 7011-23.