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Results: 1-12 |
Results: 12
The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O-2 binding pocket
Authors: Farmer, CS Kurtz, DM Liu, ZJ Wang, BC Rose, J Ai, JY Sanders-Loehr, J
Citation: Cs. Farmer et al., The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O-2 binding pocket, J BIOL I CH, 6(4), 2001, pp. 418-429
Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: Evidence for sulfur coordination in the catalytic cluster
Authors: Alvarez, ML Ai, JY Zumft, W Sanders-Loehr, J Dooley, DM
Citation: Ml. Alvarez et al., Characterization of the copper-sulfur chromophores in nitrous oxide reductase by resonance Raman spectroscopy: Evidence for sulfur coordination in the catalytic cluster, J AM CHEM S, 123(4), 2001, pp. 576-587
A leucine residue "gates" solvent but not O-2 access to the binding pocketof Phascolopsis gouldii hemerythrin
Authors: Farmer, CS Kurtz, DM Phillips, RS Ai, JY Sanders-Loehr, J
Citation: Cs. Farmer et al., A leucine residue "gates" solvent but not O-2 access to the binding pocketof Phascolopsis gouldii hemerythrin, J BIOL CHEM, 275(22), 2000, pp. 17043-17050
The catalytic center in nitrous oxide reductase, Cu-z, is a copper-sulfidecluster
Authors: Rasmussen, T Berks, BC Sanders-Loehr, J Dooley, DM Zumft, WG Thomson, AJ
Citation: T. Rasmussen et al., The catalytic center in nitrous oxide reductase, Cu-z, is a copper-sulfidecluster, BIOCHEM, 39(42), 2000, pp. 12753-12756
Resonance Raman studies of the stoichiometric catalytic turnover of a substrate-stearoyl-acyl carrier protein Delta(9) desaturase complex
Authors: Lyle, KS Moenne-Loccoz, P Ai, JY Sanders-Loehr, J Loehr, TM Fox, BG
Citation: Ks. Lyle et al., Resonance Raman studies of the stoichiometric catalytic turnover of a substrate-stearoyl-acyl carrier protein Delta(9) desaturase complex, BIOCHEM, 39(34), 2000, pp. 10507-10513
The O-2 binding pocket of myohemerythrin: Role of a conserved leucine
Authors: Xiong, JJ Phillips, RS Kurtz, DM Jin, S Ai, JY Sanders-Loehr, J
Citation: Jj. Xiong et al., The O-2 binding pocket of myohemerythrin: Role of a conserved leucine, BIOCHEM, 39(29), 2000, pp. 8526-8536
Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant
Authors: Liu, HB Zhu, HN Eggers, DK Nersissian, AM Faull, KF Goto, JJ Ai, JY Sanders-Loehr, J Gralla, EB Valentine, JS
Citation: Hb. Liu et al., Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant, BIOCHEM, 39(28), 2000, pp. 8125-8132
Reassessment of the active site quino-cofactor proposed to occur in the Aspergillus niger amine oxidase AO-I from the properties of model compounds
Authors: Melville, CR Green, EL Sanders-Loehr, J Klinman, JP
Citation: Cr. Melville et al., Reassessment of the active site quino-cofactor proposed to occur in the Aspergillus niger amine oxidase AO-I from the properties of model compounds, BIOCHEM, 39(25), 2000, pp. 7589-7594
A hemerythrin-like domain in a bacterial chemotaxis protein
Authors: Xiong, JJ Kurtz, DM Ai, JY Sanders-Loehr, J
Citation: Jj. Xiong et al., A hemerythrin-like domain in a bacterial chemotaxis protein, BIOCHEM, 39(17), 2000, pp. 5117-5125
Loop-directed mutagenesis of the blue copper protein amicyanin from Paracoccus versutus and its effect on the structure and the activity of the type-1 copper site
Authors: Buning, C Canters, GW Comba, P Dennison, C Jeuken, L Melter, M Sanders-Loehr, J
Citation: C. Buning et al., Loop-directed mutagenesis of the blue copper protein amicyanin from Paracoccus versutus and its effect on the structure and the activity of the type-1 copper site, J AM CHEM S, 122(2), 2000, pp. 204-211
An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha
Authors: Plastino, J Green, EL Sanders-Loehr, J Klinman, JP
Citation: J. Plastino et al., An unexpected role for the active site base in cofactor orientation and flexibility in the copper amine oxidase from Hansenula polymorpha, BIOCHEM, 38(26), 1999, pp. 8204-8216
Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase fromyeast
Authors: Schwartz, B Green, EL Sanders-Loehr, J Klinman, JP
Citation: B. Schwartz et al., Relationship between conserved consensus site residues and the productive conformation for the TPQ cofactor in a copper-containing amine oxidase fromyeast, BIOCHEM, 37(47), 1998, pp. 16591-16600
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