| Characterization of 3-ketosteroid 9{alpha}-hydroxylase, a rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis. Capyk J.K., D'Angelo I., Strynadka N.C., Eltis L.D.
J. Biol. Chem. 284:9937-9946(2009) · Mapped (1) |
| Determining Rieske cluster reduction potentials. Brown E.N., Friemann R., Karlsson A., Parales J.V., Couture M.M., Eltis L.D., Ramaswamy S.
J. Biol. Inorg. Chem. 13:1301-1313(2008) · Mapped (1) |
| Structure of HsaD, a steroid-degrading hydrolase, from Mycobacterium tuberculosis. Lack N., Lowe E.D., Liu J., Eltis L.D., Noble M.E., Sim E., Westwood I.M.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64:2-7(2008) · Mapped (1) |
| The molecular basis for inhibition of BphD, a C-C bond hydrolase involved in polychlorinated biphenyls degradation: large 3-substituents prevent tautomerization. Bhowmik S., Horsman G.P., Bolin J.T., Eltis L.D.
J. Biol. Chem. 282:36377-36385(2007) · UniProtKB (1) |
| The tautomeric half-reaction of BphD, a C-C bond hydrolase. Kinetic and structural evidence supporting a key role for histidine 265 of the catalytic triad. Horsman G.P., Bhowmik S., Seah S.Y., Kumar P., Bolin J.T., Eltis L.D.
J. Biol. Chem. 282:19894-19904(2007) · UniProtKB (1) |
| Characterization of a C-C bond hydrolase from Sphingomonas wittichii RW1 with novel specificities towards polychlorinated biphenyl metabolites. Seah S.Y., Ke J., Denis G., Horsman G.P., Fortin P.D., Whiting C.J., Eltis L.D.
J. Bacteriol. 189:4038-4045(2007) · UniProtKB (2) |
| Crystal structures reveal an induced-fit binding of a substrate-like Aza-peptide epoxide to SARS coronavirus main peptidase. Lee T.W., Cherney M.M., Liu J., James K.E., Powers J.C., Eltis L.D., James M.N.
J. Mol. Biol. 366:916-932(2007) · Mapped (2) |
| The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse. McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D. et al.
Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) · UniProtKB (9,075) |
| Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway. Horsman G.P., Ke J., Dai S., Seah S.Y.K., Bolin J.T., Eltis L.D.
Biochemistry 45:11071-11086(2006) · UniProtKB (1) |
| Structures of ternary complexes of BphK, a bacterial glutathione S-transferase that reductively dechlorinates polychlorinated biphenyl metabolites. Tocheva E.I., Fortin P.D., Eltis L.D., Murphy M.E.
J. Biol. Chem. 281:30933-30940(2006) · Mapped (1) |
| An episulfide cation (thiiranium ring) trapped in the active site of HAV 3C proteinase inactivated by peptide-based ketone inhibitors. Yin J., Cherney M.M., Bergmann E.M., Zhang J., Huitema C., Pettersson H., Eltis L.D., Vederas J.C., James M.N.G.
J. Mol. Biol. 361:673-686(2006) · UniProtKB (1) · Mapped (1) |
| Identification and analysis of a bottleneck in PCB biodegradation. Dai S., Vaillancourt F.H., Maaroufi H., Drouin N.M., Neau D.B., Snieckus V., Bolin J.T., Eltis L.D.
Nat. Struct. Biol. 9:934-939(2002) · Mapped (1) |
| A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Colbert C.L., Couture M.M.-J., Eltis L.D., Bolin J.T.
Structure 8:1267-1278(2000) · UniProtKB (1) · Mapped (3) |
| Characterization of BphF, a Rieske-type ferredoxin with a low reduction potential. Couture M.M.-J., Colbert C.L., Babini E., Rosell F.I., Mauk A.G., Bolin J.T., Eltis L.D.
Biochemistry 40:84-92(2001) · UniProtKB (1) |
| Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl 1,2-dioxygenase by t-butanol. Vaillancourt F.H., Han S., Fortin P.D., Bolin J.T., Eltis L.D.
J. Biol. Chem. 273:34887-34895(1998) · UniProtKB (1) · Mapped (2) |
| Crystal structure of cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase from a PCB degrader at 2.0-A resolution. Huelsmeyer M., Hecht H.-J., Niefind K., Hofer B., Eltis L.D., Timmis K.N., Schomburg D.
Protein Sci. 7:1286-1293(1998) · UniProtKB (1) |
| The solution structure refinement of the paramagnetic reduced high-potential iron-sulfur protein I from Ectothiorhodospira halophila by using stable isotope labeling and nuclear relaxation. Bertini I., Couture M.M.J., Donaire A., Eltis L.D., Felli I.C., Luchinat C., Piccioli M., Rosati A.
Eur. J. Biochem. 241:440-452(1996) · UniProtKB (1) |
| Purification and characterization of cytochrome P450RR1 from Rhodococcus rhodochrous. Eltis L.D., Karlson U., Timmis K.N.
Eur. J. Biochem. 213:211-216(1993) · UniProtKB (1) |
| Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase. Eltis L.D., Hofmann B., Hecht H.J., Luensdorf H., Timmis K.N.
J. Biol. Chem. 268:2727-2732(1993) · UniProtKB (1) |
| Effects of charged amino acid mutations on the bimolecular kinetics of reduction of yeast iso-1-ferricytochrome c by bovine ferrocytochrome b5. Northrup S.H., Thomasson K.A., Miller C.M., Barker P.D., Eltis L.D., Guillemette J.G., Inglis S.C., Mauk A.G.
Biochemistry 32:6613-6623(1993) · Mapped (1) |
| Genetic analysis of a Pseudomonas locus encoding a pathway for biphenyl/polychlorinated biphenyl degradation. Hofer B., Eltis L.D., Dowling D.N., Timmis K.N.
Gene 130:47-55(1993) · UniProtKB (3) |
| Characterization of 2,2',3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1. Happe B., Eltis L.D., Poth H., Hedderich R., Timmis K.N.
J. Bacteriol. 175:7313-7320(1993) · UniProtKB (12) |
| Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases. Asturias J.A., Eltis L.D., Prucha M., Timmis K.N.
J. Biol. Chem. 269:7807-7815(1994) · UniProtKB (4) |
| The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance. Banci L., Bertini I., Eltis L.D., Felli I.C., Kastrau D.H.W., Luchinat C., Piccioli M., Pierattelli R., Smith M.
Eur. J. Biochem. 225:715-725(1994) · UniProtKB (1) |
| Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. Guillemette J.G., Barker P.D., Eltis L.D., Lo T.P., Smith M., Brayer G.D., Mauk A.G.
Biochimie 76:592-604(1994) · Mapped (2) |
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