Understanding heme cavity structure of peroxidases: comparison of electronic absorption and resonance Raman spectra with crystallographic results.
Electronic absorption and resonance Raman spectra of various peroxidases and selected site-directed mutants are reported. These results and the X-ray crystal structure data are critically analyzed and underline the differences that exist between the crystal and solution states. The effect of the vinyl conjugation on the electronic absorption maxima and the influence of the ligand nature on the wavelength of the charge-transfer (CT1) band are shown to be useful probes of subtle interactions in the heme pocket. The spectroscopic differences observed between the three classes of peroxidases are discussed in terms of their structural diversity.
Smulevich
G
G
Dipartimento di Chimica, Universitá di Firenze, Italy. smulev@chim.unifi.it
D001665:Binding Sites / Q000235:genetics; D018360:Crystallography, X-Ray; D006418:Heme / Q000737:chemistry* / Q000235:genetics; D006420:Hemeproteins / Q000737:chemistry; D008024:Ligands; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010544:Peroxidases / Q000737:chemistry* / Q000145:classification / Q000235:genetics; D011487:Protein Conformation; D013057:Spectrum Analysis; D013059:Spectrum Analysis, Raman; D014965:X-Rays
D006420:Hemeproteins; D008024:Ligands; D006418:Heme; D010544:Peroxidases