High-resolution proton nuclear magnetic resonance spectroscopy of chloride peroxidase: identification of new forms of the enzyme
Chloride peroxidase from the mold Caldariomyces fumago in the native high-spin iron(III) and low-spin cyanoiron (III) states has been subjected to high-field proton nuclear magnetic resonance spectroscopic measurements. Signals shifted well outside the diamagnetic envelope by the paramagnetic iron(III) center are surprisingly insensitive to pH changes over the range from pH 3 to pH 7. The previously identified major form of chloride peroxidase (form A) and the minor form (B) show very similar chemical shift patterns. Of greatest significance, however, is the discovery that each of the separable forms of the enzyme exhibits splitting of porphyrin ring methyl resonances. The appearance of two sets of signals in both native and cyanide-complexed enzyme is best explained by the existence of two additional forms of the A and B isoenzymes. Structural differences for the newly identified forms of chloride peroxidase must be located in the vicinity of the heme prosthetic group.
- OSTI ID:
- 5128252
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 4; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
400104 -- Spectral Procedures-- (-1987)
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
CARBOXYLIC ACIDS
COMPLEXES
CYANIDES
DEUTERIUM
ENZYMES
FUNGI
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HYDROGEN COMPOUNDS
HYDROGEN ISOTOPES
IRON COMPLEXES
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ODD-ODD NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDOREDUCTASES
OXYGEN COMPOUNDS
PEROXIDASES
PH VALUE
PLANTS
PORPHYRINS
RESONANCE
STABLE ISOTOPES
TRANSITION ELEMENT COMPLEXES
WATER