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Results: 1-7 |
Results: 7
Investigations of the roles of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin
Authors: Ozaki, SI Roach, MP Matsui, T Watanabe, Y
Citation: Si. Ozaki et al., Investigations of the roles of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin, ACC CHEM RE, 34(10), 2001, pp. 818-825
Proximal ligand control of heme iron coordination structure and reactivitywith hydrogen peroxide: investigations of the myoglobin cavity mutant H93Gwith unnatural oxygen donor proximal ligands
Authors: Roach, MP Puspita, WJ Watanabe, Y
Citation: Mp. Roach et al., Proximal ligand control of heme iron coordination structure and reactivitywith hydrogen peroxide: investigations of the myoglobin cavity mutant H93Gwith unnatural oxygen donor proximal ligands, J INORG BIO, 81(3), 2000, pp. 173-182
The H93G myoglobin cavity mutant as a versatile template for modeling hemeproteins: Ferrous, ferric, and ferryl mixed-ligand complexes with imidazole in the cavity
Authors: Pond, AE Roach, MP Thomas, MR Boxer, SG Dawson, JH
Citation: Ae. Pond et al., The H93G myoglobin cavity mutant as a versatile template for modeling hemeproteins: Ferrous, ferric, and ferryl mixed-ligand complexes with imidazole in the cavity, INORG CHEM, 39(26), 2000, pp. 6061-6066
Rational molecular design of a catalytic site: engineering of catalytic functions to the myoglobin active site framework
Authors: Ozaki, S Matsui, T Roach, MP Watanabe, Y
Citation: S. Ozaki et al., Rational molecular design of a catalytic site: engineering of catalytic functions to the myoglobin active site framework, COORD CH RE, 198, 2000, pp. 39-59
Investigations of the myoglobin cavity mutant H93G with unnatural imidazole proximal ligands as a modular peroxide O-O bond cleavage model system
Authors: Roach, MP Ozaki, S Watanabe, Y
Citation: Mp. Roach et al., Investigations of the myoglobin cavity mutant H93G with unnatural imidazole proximal ligands as a modular peroxide O-O bond cleavage model system, BIOCHEM, 39(6), 2000, pp. 1446-1454
Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) andheme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism
Authors: Pond, AE Roach, MP Sono, M Rux, AH Franzen, S Hu, R Thomas, MR Wilks, A Dou, Y Ikeda-Saito, M de Montelano, PRO Woodruff, WH Boxer, SG Dawson, JH
Citation: Ae. Pond et al., Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) andheme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism, BIOCHEM, 38(23), 1999, pp. 7601-7608
The role of the distal and proximal protein environments in controlling the ferric spin state and in stabilizing thiolate ligation in heme systems: Thiolate adducts of the myoglobin H93G cavity mutant
Authors: Roach, MP Pond, AE Thomas, MR Boxer, SG Dawson, JH
Citation: Mp. Roach et al., The role of the distal and proximal protein environments in controlling the ferric spin state and in stabilizing thiolate ligation in heme systems: Thiolate adducts of the myoglobin H93G cavity mutant, J AM CHEM S, 121(51), 1999, pp. 12088-12093
Risultati: 1-7 |