MOSSBAUER INVESTIGATIONS OF CHLOROPEROXIDASE AND ITS HALIDE COMPLEXES
MOSSBAUER INVESTIGATIONS OF CHLOROPEROXIDASE AND ITS HALIDE COMPLEXES
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DOI：
10.1021/bi00727a011
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发表时间：
1973-01-01
期刊：
影响因子：
2.9
通讯作者：
HAGER, LP
中科院分区：
文献类型：
--
作者：
CHAMPION, PM;MUNCK, E;HAGER, LP
P. M. Champion, E. Münck, P. G. Debrunner, P. F. Hollenberg, and L. P. Hager abstract: The heme protein chloroperoxidase which is isolated from the mold Caldariomyces fumago has been investigated by Mossbauer spectroscopy. The heme iron of native chloroperoxidase is in a low-spin ferric state at low tempera-tures and undergoes a temperature-dependent spin transition to high-spin ferric around 200 K. The low-temperature Mossbauer spectra were simulated assuming that the heme iron resides in a ligand field potential of orthorhombic symmetry. The low-temperature Mossbauer spectra of the chloroperoxidasc-Cl complex are quite similar to those of the native enzyme, suggesting that chloride does not bind as an axial ligand to the heme iron. The complexes of chloroperoxidase with iodide and fluoride are high-spin ferric at all tempera-cX^ Vhloroperoxidase is a heme protein (mol wt~42,000) which has been isolated from the mold Caldariomyces fumago (Morris and Hager, 1966). It catalyzes the chlorination reac-tions involved in the biosynthesis of caldariomycin (2, 2-dichloro-1, 3-cyclopentenedione). In the presence of hydrogen peroxide and a suitable halogen donor (I-, Br “, or Cl”, but not F”), the enzyme catalyzes the peroxidativeformation of a carbon-halogen bond with a suitable halogen acceptor. In
