Distal Heme Pocket Mutant (R38S/H42E) of Recombinant Horseradish Peroxidase C (HRP C).

Structural analysis of the two horseradish peroxidase catalytic residue variants H42E and R38S/H42E: implications for the catalytic cycle.

Crystal structure of horseradish peroxidase C at 2.15 A resolution.

Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography.

The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates.

QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILSLHFEDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPVI
DRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNRS
SDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQ
KGLIQSDQELFSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVNSNS

PEG-8000, calcium acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K

Wild type crystallised in space group P3112

Wild type crystallised in space group P212121 in complex with ferulic acid

Active site mutant (H42E) crystallised in space group P21 in complex with benzhydroxamic acid

Heme ligand mutant (F221M) crystallised in space group P21 in complex with benzhydroxamic acid

THE NORMAL S-S BRIDGE BETWEEN CYS97 AND CYS301 HAS BEEN BROKEN AS A RESULT OF RADIATION DAMAGE.

PDB entry 6atj without water was used as a starting model.

Peroxidase, Oxidoreductase, Horseradish, Heme enzyme, Mutant

QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCDASILLDNTTSFRTEKDAFGNANSARGFPVI
DRMKAAVESACPRTVSCADLLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKDSFRNVGLNRS
SDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTTYLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQ
KGLIQSDQELFSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLNCRVVNSNS