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1
Reactions of ligands with heme-substituted horseradish ferroperoxidases.
Biochim Biophys Acta. 1973 Oct 18;322(2):211-7. doi: 10.1016/0005-2795(73)90295-x.
2
Heme-modification studies on horseradish peroxidase.
Biochim Biophys Acta. 1972 May 12;268(2):292-304. doi: 10.1016/0005-2744(72)90324-5.
3
Effects of 2,4-substituents of deuteroheme upon peroxidase functions. Reactions of peroxidase and myoglobin with oxygen, carbon monoxide and alkylisocyanides.
Arch Biochem Biophys. 1974 Dec;165(2):485-93. doi: 10.1016/0003-9861(74)90274-4.
4
Diffusion-controlled reaction kinetics of the binding of carbon monoxide to the heme undecapeptide of cytochrome c (microperoxidase 11) in high viscosity solvents.
Arch Biochem Biophys. 1981 Oct 1;211(1):396-402. doi: 10.1016/0003-9861(81)90470-7.
5
Effects of 2,4-substituents of deuteroheme upon peroxidase functions. II. Reactions of peroxidases and metmyoglobin with azide, cyanide and fluoride.
Arch Biochem Biophys. 1973 Aug;157(2):356-68. doi: 10.1016/0003-9861(73)90650-4.
6
A search for a leghaemoglobin-like compound in root nodules of Trema cannabina Lour.
Biochim Biophys Acta. 1976 Jan 20;420(1):105-11. doi: 10.1016/0005-2795(76)90349-4.
7
Heme-linked protonation of HCN, CO, NO and O2 complexes of reduced horseradish peroxidases.
Arch Biochem Biophys. 1975 Dec;171(2):737-44. doi: 10.1016/0003-9861(75)90087-9.
8
Studies on the equilibria and kinetics of the reactions of peroxidases with ligands. I. The reaction of ferroperoxidases with carbon monoxide.
Biochemistry. 1965 Dec;4(12):2672-6. doi: 10.1021/bi00888a016.
9
Effect of heme-apoprotein interactions on the activity of horseradish and wheat germ peroxidases.
Biochem Biophys Res Commun. 1994 Oct 14;204(1):1-6. doi: 10.1006/bbrc.1994.2417.
10
Circular dichroism and absorption spectra of horse radish peroxidase and sperm whale myoglobin in the Soret region.
Biochemistry. 1969 Sep;8(9):3729-34. doi: 10.1021/bi00837a036.
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