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Characterization of the spontaneous "aging" of the heme oxygenase from the pathological bacterium Neisseria meningitidis via cleavage of the C-terminus in contact with the substrate. Implications for functional studies and the crystal structure.
Liu Y, Ma LH, Zhang X, Yoshida T, Satterlee JD, La Mar GN. Liu Y, et al. Among authors: la mar gn. Biochemistry. 2006 Mar 28;45(12):3875-86. doi: 10.1021/bi0523097. Biochemistry. 2006. PMID: 16548515 Free PMC article.
Modulation of the axial water hydrogen-bonding properties by chemical modification of the substrate in resting state, substrate-bound heme oxygenase from Neisseria meningitidis; coupling to the distal H-bond network via ordered water molecules.
Ma LH, Liu Y, Zhang X, Yoshida T, Langry KC, Smith KM, La Mar GN. Ma LH, et al. Among authors: la mar gn. J Am Chem Soc. 2006 May 17;128(19):6391-9. doi: 10.1021/ja0578505. J Am Chem Soc. 2006. PMID: 16683803 Free PMC article.
1H NMR Study of the influence of hemin vinyl-->methyl substitution on the interaction between the C-terminus and substrate and the "aging" of the heme oxygenase from Neisseria meningitidis: induction of active site structural heterogeneity by a two-fold symmetric hemin.
Liu Y, Ma LH, Zhang X, Yoshida T, Satterlee JD, La Mar GN. Liu Y, et al. Among authors: la mar gn. Biochemistry. 2006 Nov 21;45(46):13875-88. doi: 10.1021/bi061747q. Biochemistry. 2006. PMID: 17105206
191 results