Proton nuclear Overhauser effect study of the heme active site structure of Coprinus macrorhizus peroxidase.
Proton nuclear Overhauser effect and paramagnetic relaxation measurements have been used to define more extensively the heme active site structure of Coprinus macrorhizus peroxidase, CMP (previously known as Coprinus cinereus peroxidase), as the ferric low-spin cyanide ligated complex. The results are compared with other well-characterized peroxidase enzymes. The NMR spectrum of CMPCN shows changes in the paramagnetically shifted resonances as a function of time, suggesting a significant heme disorder for CMP. The presence of proximal and distal histidine amino acid residues are common to the heme environments of both CMPCN and HRPCN. However, the upfield distal arginine signals of HRPCN are not evident in the 1H-NMR spectra of CMPCN.
Dugad
L B
LB
Department of Chemistry, University of Iowa, Iowa City 52242.
Goff
H M
HM
D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003302:Coprinus / Q000201:enzymology*; D003578:Cytochrome-c Peroxidase / Q000737:chemistry; D006418:Heme / Q000737:chemistry*; D006639:Histidine; D006735:Horseradish Peroxidase / Q000737:chemistry; D006877:Hydroxamic Acids / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009195:Peroxidase / Q000737:chemistry*
D006877:Hydroxamic Acids; D006418:Heme; D006639:Histidine; D006735:Horseradish Peroxidase; D003578:Cytochrome-c Peroxidase; D009195:Peroxidase; C006696:benzohydroxamic acid