Characterization of the siroheme active site in spinach nitrite reductase by resonance Raman spectroscopy.
The resonance Raman spectra of various species of spinach nitrite reductase (ferredoxin: nitrite oxidoreductase, EC 1.7.7.1) have been obtained with Soret excitation. These spectra allow for the vibrational properties of the unique siroheme chromophore at the enzyme's active site. The wholesale reordering of siroheme vibrational properties relative to those of protoporphyrins can be rationalized as resulting from a combination of symmetry lowering and bond order reductions within the siroheme macrocyle.
D001665:Binding Sites; D006418:Heme / Q000031:analogs & derivatives* / Q000032:analysis; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis*; D009572:Nitrite Reductases / Q000032:analysis*; D010944:Plants / Q000201:enzymology*; D013059:Spectrum Analysis, Raman
D006418:Heme; C009272:siroheme; D009247:NADH, NADPH Oxidoreductases; D009572:Nitrite Reductases