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Low‐temperature magnetic circular dichroism investigation of the active site of chloroperoxidase
Author(s) -
Yarmola Elena G.,
Sharonov Yurii A.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01206-7
Subject(s) - chemistry , magnetic circular dichroism , heme , circular dichroism , photodissociation , carbon monoxide , active site , photochemistry , cytochrome , substrate (aquarium) , crystallography , spectral line , enzyme , organic chemistry , catalysis , physics , oceanography , astronomy , geology
Magnetic circular dichroism (MCD) spectra for near UV and visible spectral regions of chemically reduced chloroperoxidase from Caldariomyces fumago have been recorded at temperatures from near 293 to 2.15 K. The spectra of reduced chloroperoxidase at 4.2 K were compared with those of photolysis products of its carbon monoxide complexes. Obtained results give evidence for high rigidity of the active site in chloroperoxidase and strongly suggest that thiolate is a protein‐derived ligand of the heme iron in the reduced enzyme. The unusual high‐spin ferrohemoproteins temperature dependence of the Soret MCD closely resembles that of the substrate‐bound cytochrome P‐450 cam .