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EC Number
Metals/Ions
Commentary
Reference
Ca2+
a single, tightly bound, Ca2+ ion at the domain interface of both the fully oxidized and mixed-valence forms of the enzyme is absolutely required for catalytic activity, reduction of the electron-transferring (high-potential) heme in the presence of Ca2+ ions triggers substantial structural rearrangements around the active-site (low-potential) heme to allow substrate binding and catalysis
Ca2+
pre-incubation with the cation has no effect on activity
Ca2+
with added Ca2+, the peroxidatic heme is five-coordinate high-spin and active
Fe
2 hemes
Fe
2 hemes per subunit
Fe
static titration of ferric cytochrome c peroxidase with reduced azurin shows that only one of the two hemes in the enzyme seems to be readily reduced
Fe
two haeme groups
Fe
two haemes per monomer, pyridine haemochrome spectra
Fe2+
diheme cytochrome c peroxidase
Fe2+
heme
Results 1 - 10 of 18 > >>