Dependence of heme accessibility in horseradish peroxidase on Ca2
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[1] D. Converso,et al. Ca2+ activation of wheat peroxidase: a possible physiological mechanism of control. , 1996, Archives of biochemistry and biophysics.
[2] D. J. Schuller,et al. The crystal structure of peanut peroxidase. , 1996, Structure.
[3] Anant B. Patel,et al. Spectroscopic studies on calcium depleted horseradish peroxidase: Observation of tryptophan sensitized bound terbium(III) flourescence , 1995 .
[4] Q. Zhang,et al. Heme protein dynamics studied by phosphorescence of an external phosphorescent probe molecule. , 1994, Archives of biochemistry and biophysics.
[5] S. Hamai. Room-temperature phosphorescence of 6-bromo-2-naphthol included by α-cyclodextrin in aqueous solution , 1994 .
[6] G. Hernández,et al. H NMR investigation of the influence of interacting sites on the dynamics and thermodynamics of substrate and ligand binding to horseradish peroxidase. , 1992, Biochemistry.
[7] S A Sanders,et al. Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41----Val, with altered reactivity towards hydrogen peroxide and reducing substrates. , 1992, European journal of biochemistry.
[8] M. Schuh,et al. DEMONSTRATION THAT PHOSPHORESCENT 6‐BROMO‐2‐NAPHTHYL SULFATE CAN BE USED TO PROBE HEME ACCESSIBILITY IN HEME PROTEINS , 1991, Photochemistry and photobiology.
[9] J. Feitelson,et al. Diffusion of small molecules through the structure of myoglobin. Environmental effects. , 1989, Biochemistry.
[10] W. Caughey,et al. Bovine myeloperoxidase and lactoperoxidase each contain a high affinity site for calcium. , 1989, Biochemical and biophysical research communications.
[11] E. Pines,et al. Geminate recombination in proton‐transfer reactions. II. Comparison of diffusional and kinetic schemes , 1988 .
[12] J. Feitelson,et al. Quenching of the zinc-protoporphyrin triplet state as a measure of small-molecule diffusion through the structure of myoglobin. , 1987, Biochemistry.
[13] R. Chibbar,et al. Ca2+ and peroxidase derived from cultured peanut cells , 1987 .
[14] S. Takahashi,et al. Nuclear magnetic resonance studies on the spatial relationship of aromatic donor molecules to the heme iron of horseradish peroxidase. , 1986, The Journal of biological chemistry.
[15] H. Greppin,et al. Molecular and physiological aspects of plant peroxidases , 1986 .
[16] B C Finzel,et al. Crystal structure of yeast cytochrome c peroxidase refined at 1.7-A resolution. , 1984, The Journal of biological chemistry.
[17] M. Kato,et al. Isolation and characterization of five neutral isoenzymes of horseradish peroxidase. , 1982, Journal of biochemistry.
[18] N. Turro,et al. A STUDY OF THE KINETICS OF INCLUSION OF HALONAPHTHALENES WITH ß‐CYCLODEXTRIN VIA TIME CORRELATED PHOSPHORESCENCE , 1982 .
[19] I. Aviram. The interaction of benzhydroxamic acid with horseradish peroxidase and its fluorescent analogs. , 1981, Archives of biochemistry and biophysics.
[20] I. Morishima,et al. Calcium binding by horseradish peroxidase C and the heme environmental structure. , 1979, Biochemical and biophysical research communications.
[21] R. Haschke,et al. Calcium-related properties of horseradish peroxidase. , 1978, Biochemical and biophysical research communications.
[22] G. R. Schonbaum. New complexes of peroxidases with hydroxamic acids, hydrazides, and amides. , 1973, The Journal of biological chemistry.
[23] L. Shannon,et al. Peroxidase isozymes from horseradish roots. I. Isolation and physical properties. , 1966, The Journal of biological chemistry.
[24] E. Breslow. CHANGES IN SIDE CHAIN REACTIVITY ACCOMPANYING THE BINDING OF HEME TO SPERM WHALE APOMYOGLOBIN. , 1964, The Journal of biological chemistry.