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NMR study of the active site of resting state and cyanide-inhibited lignin peroxidase from Phanerochaete chrysosporium. Comparison with horseradish peroxidase.
de Ropp JS, La Mar GN, Wariishi H, Gold MH. de Ropp JS, et al. J Biol Chem. 1991 Aug 15;266(23):15001-8. J Biol Chem. 1991. PMID: 1869537 Free article.
In contrast, the absence of any resolved signals attributable to an Arg44 in LiP-CN suggest that this distal residue has an altered orientation relative to the heme compared with that of the conserved Arg38 in HRP-CN (Thanabal, V., de Ropp, J. S., and La Mar, …
In contrast, the absence of any resolved signals attributable to an Arg44 in LiP-CN suggest that this distal residue has an altered orientat …
Identification of residues in the aromatic substrate binding site of horseradish peroxidase by 1H NMR studies on isozymes.
de Ropp JS, Chen Z, Mar GN. de Ropp JS, et al. Biochemistry. 1995 Oct 17;34(41):13477-84. doi: 10.1021/bi00041a027. Biochemistry. 1995. PMID: 7577936
The cyanide-inhibited complexes of two horseradish peroxidase acidic isozymes, A1 (HRPA1, unsequenced) and A2 (HRPA2, sequenced), have been examined by solution two-dimensional 1H NMR methods, and the active site molecular and electronic structure compared to that of the well-cha …
The cyanide-inhibited complexes of two horseradish peroxidase acidic isozymes, A1 (HRPA1, unsequenced) and A2 (HRPA2, sequenced), have been …
26 results