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Results: 1-16 |
Results: 16
Solution H-1 NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase - Comparison to the crystal structure of the water-ligated form
Authors: La Mar, GN Asokan, A Espiritu, B Yeh, DC Auclair, K de Montellano, PRO
Citation: Gn. La Mar et al., Solution H-1 NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase - Comparison to the crystal structure of the water-ligated form, J BIOL CHEM, 276(19), 2001, pp. 15676-15687
Solution NMR characterization of the thermodynamics of the disulfide bond orientational isomerism and its effect of cluster electronic properties forthe hyperthermostable three-iron cluster ferredoxin from the archaeon Pyrococcus furiosus
Authors: da Silva, MW Sham, S Gorst, CM Calzolai, L Brereton, PS Adams, MWW La Mar, GN
Citation: Mw. Da Silva et al., Solution NMR characterization of the thermodynamics of the disulfide bond orientational isomerism and its effect of cluster electronic properties forthe hyperthermostable three-iron cluster ferredoxin from the archaeon Pyrococcus furiosus, BIOCHEM, 40(42), 2001, pp. 12575-12583
H-1 and C-13 NMR investigation of the influence of nonligated residue contacts on the heme electronic structure in cyanometmyoglobin complexes reconstituted with centro- and pseudocentrosymmetric hemins
Authors: Hu, B Hauksson, JB Tran, ATT Kolczak, U Pandey, RK Rezzano, IN Smith, KM La Mar, GN
Citation: B. Hu et al., H-1 and C-13 NMR investigation of the influence of nonligated residue contacts on the heme electronic structure in cyanometmyoglobin complexes reconstituted with centro- and pseudocentrosymmetric hemins, J AM CHEM S, 123(41), 2001, pp. 10063-10070
Solution NMR determination of the seating(s) of meso-nitro-etioheme-1 in myoglobin: Implications for steric constraints to meso position access in heme degradation by coupled oxidation
Authors: Wang, JT Li, YM Ma, DJ Kalish, H Balch, AL La Mar, GN
Citation: Jt. Wang et al., Solution NMR determination of the seating(s) of meso-nitro-etioheme-1 in myoglobin: Implications for steric constraints to meso position access in heme degradation by coupled oxidation, J AM CHEM S, 123(33), 2001, pp. 8080-8088
A gallium-substituted cubane-type cluster in Pyrococcus furiosus ferredoxin
Authors: Johnson, KA Brereton, PS Verhagen, MFJM Calzolai, L La Mar, GN Adams, MWW Amster, IJ
Citation: Ka. Johnson et al., A gallium-substituted cubane-type cluster in Pyrococcus furiosus ferredoxin, J AM CHEM S, 123(32), 2001, pp. 7935-7936
Solution H-1 NMR of the molecular and electronic structure of the heme cavity and substrate binding pocket of high-spin ferric horseradish peroxidase: Effect of His42Ala mutation
Authors: Asokan, A de Ropp, JS Newmyer, SL de Montellano, PRO La Mar, GN
Citation: A. Asokan et al., Solution H-1 NMR of the molecular and electronic structure of the heme cavity and substrate binding pocket of high-spin ferric horseradish peroxidase: Effect of His42Ala mutation, J AM CHEM S, 123(18), 2001, pp. 4243-4254
Solution H-1 NMR characterization of axial interactions of the proximal and distal His in the cyanomet complexes of the isolated chains and the 65 kDa intact tetramer of human hemoglobin A
Authors: La Mar, GN Kolczak, U Tran, ATT Chien, EYT
Citation: Gn. La Mar et al., Solution H-1 NMR characterization of axial interactions of the proximal and distal His in the cyanomet complexes of the isolated chains and the 65 kDa intact tetramer of human hemoglobin A, J AM CHEM S, 123(18), 2001, pp. 4266-4274
Solution H-1 NMR investigation of the seating and rotational "hopping" of centrosymmetric etioheme-I in myoglobin: effect of globin origin and its oxidation/spin state on heme dynamics
Authors: Tran, ATT Kalish, H Balch, AL La Mar, GN
Citation: Att. Tran et al., Solution H-1 NMR investigation of the seating and rotational "hopping" of centrosymmetric etioheme-I in myoglobin: effect of globin origin and its oxidation/spin state on heme dynamics, J BIOL I CH, 5(5), 2000, pp. 624-633
The use of chemical shift temperature gradients to establish the paramagnetic susceptibility tensor orientation: Implication for structure determination/refinement in paramagnetic metalloproteins
Authors: Xia, ZC Nguyen, BD La Mar, GN
Citation: Zc. Xia et al., The use of chemical shift temperature gradients to establish the paramagnetic susceptibility tensor orientation: Implication for structure determination/refinement in paramagnetic metalloproteins, J BIOM NMR, 17(2), 2000, pp. 167-174
Solution H-1 NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin
Authors: Nguyen, BD Xia, ZC Cutruzzola, F Allocatelli, CT Brunori, R La Mar, GN
Citation: Bd. Nguyen et al., Solution H-1 NMR study of the influence of distal hydrogen bonding and N terminus acetylation on the active site electronic and molecular structure of Aplysia limacina cyanomet myoglobin, J BIOL CHEM, 275(2), 2000, pp. 742-751
Solution H-1 NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune
Authors: Yeh, DC Thorsteinsson, MV Bevan, DR Potts, M La Mar, GN
Citation: Dc. Yeh et al., Solution H-1 NMR study of the heme cavity and folding topology of the abbreviated chain 118-residue globin from the cyanobacterium Nostoc commune, BIOCHEM, 39(6), 2000, pp. 1389-1399
H-1 NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin
Authors: Xia, ZC Zhang, W Nguyen, BD La Mar, GN Kloek, AP Goldberg, DE
Citation: Zc. Xia et al., H-1 NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris suum hemoglobin, J BIOL CHEM, 274(45), 1999, pp. 31819-31826
Solution H-1 NMR investigation of the heme cavity and substrate binding site in cyanide-inhibited horseradish peroxidase
Authors: de Ropp, JS Mandal, PK La Mar, GN
Citation: Js. De Ropp et al., Solution H-1 NMR investigation of the heme cavity and substrate binding site in cyanide-inhibited horseradish peroxidase, BIOCHEM, 38(3), 1999, pp. 1077-1086
Secondary structure extensions in Pyrococcus furiosus ferredoxin destabilize the disulfide bond relative to that in other hyperthermostable ferredoxins. Global consequences for the disulfide orientational heterogeneity
Authors: Wang, PL Calzolai, L Bren, KL Teng, QC Jenney, FE Brereton, PS Howard, JB Adams, MWW La Mar, GN
Citation: Pl. Wang et al., Secondary structure extensions in Pyrococcus furiosus ferredoxin destabilize the disulfide bond relative to that in other hyperthermostable ferredoxins. Global consequences for the disulfide orientational heterogeneity, BIOCHEM, 38(25), 1999, pp. 8167-8178
H-1 NMR investigation of the role of intrinsic heme versus protein-inducedrhombic perturbations on the electronic structure of low-spin ferrihemoproteins: Effect of heme substituents on heme orientation in myoglobin
Authors: Kolczak, U Hauksson, JB Davis, NL Pande, U de Ropp, JS Langry, KC Smith, KM La Mar, GN
Citation: U. Kolczak et al., H-1 NMR investigation of the role of intrinsic heme versus protein-inducedrhombic perturbations on the electronic structure of low-spin ferrihemoproteins: Effect of heme substituents on heme orientation in myoglobin, J AM CHEM S, 121(4), 1999, pp. 835-843
Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide: Implications for the population of excited electronic states
Authors: Nguyen, BD Xia, ZC Yeh, DC Vyas, K Deaguero, H La Mar, GN
Citation: Bd. Nguyen et al., Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide: Implications for the population of excited electronic states, J AM CHEM S, 121(1), 1999, pp. 208-217
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