Resonance Raman Spectroscopic Examination of Ferrochelatase-induced Porphyrin Distortion
ferrochelatase, resonance Raman, protoporphyrin IX, heme, normal structure decomposition, tetrapyrrole, enzyme, X-ray structures
Digital Object Identifier (DOI)
Ferrochelatase, the terminal enzyme of the heme biosynthetic pathway, catalyzes the insertion of ferrous iron into protoporphyrin IX to give heme. Resonance Raman spectroscopy has been instrumental in defining the distortion (mode and extent) of the porphyrin substrate, which is a critical step in the catalytic mechanism of ferrochelatase. Saddling is the predominant porphyrin out-of-plane deformation induced upon binding to ferrochelatase. Our analysis demonstrated that the intensity of the γ15 line, which is assigned to an out-of-plane porphyrin vibration, in resonance Raman spectra obtained for wild-type- and variant ferrochelatase-bound porphyrin, correlates with the saddling deformation undergone by the porphyrin substrate. Further analysis of the three dimensional X-ray structures of bacterial, human and yeast ferrochelatases and the type and extent of distortion of the protein-bound porphyrin substrate and inhibitors using normal structure decomposition, support the view that ferrochelatase catalysis involves binding of a distorted porphyrin substrate and releasing of a flatter, metalated porphyrin.
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Citation / Publisher Attribution
World Scientific Publishing Company, v. 15, issue 5, p. 357-363
Scholar Commons Citation
Franco, Ricardo; Al-Karadaghi, Salam; and Ferreira, Gloria C., "Resonance Raman Spectroscopic Examination of Ferrochelatase-induced Porphyrin Distortion" (2011). Molecular Medicine Faculty Publications. 49.