ISSN:
1432-1327
Keywords:
Key words Peroxidase
;
Wheat germ peroxidase
;
NMR spectroscopy
;
Proximal histidine
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract The heme protein wheat germ peroxidase (isoenzyme C2) and its cyanide-inhibited form have been investigated by means of electronic, CD and paramagnetic NMR spectroscopy. The data indicate a protein environment of the active site distinct from that of horseradish peroxidase (HRP), with a larger solvent accessibility. The iron is pentacoordinated at neutral and low pH, whereas a hydroxyl anion may be bound at alkaline pH. The fifth axial ligand is a His residue with a partial anionic character, as found in other peroxidases. A spin equilibrium is observed at high enzyme concentrations.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s007750050127
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