{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T16:43:43Z","timestamp":1761237823439},"reference-count":33,"publisher":"World Scientific Pub Co Pte Lt","issue":"05n06","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Porphyrins Phthalocyanines"],"published-print":{"date-parts":[[2011,5]]},"abstract":"<jats:p> 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 \u03b3<jats:sub>15<\/jats:sub> 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. <\/jats:p>","DOI":"10.1142\/s1088424611003380","type":"journal-article","created":{"date-parts":[[2011,7,12]],"date-time":"2011-07-12T08:14:27Z","timestamp":1310458467000},"page":"357-363","source":"Crossref","is-referenced-by-count":15,"title":["Resonance Raman spectroscopic examination of ferrochelatase-induced porphyrin distortion"],"prefix":"10.1142","volume":"15","author":[{"given":"Ricardo","family":"Franco","sequence":"first","affiliation":[{"name":"REQUIMTE, Departamento de Qu\u00edmica, Faculdade de Ci\u00eancias e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal"}]},{"given":"Salam","family":"Al-Karadaghi","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Structural Biology, Lund University, Box 124, SE-22100 Lund, Sweden"}]},{"given":"Gloria C.","family":"Ferreira","sequence":"additional","affiliation":[{"name":"Department of Molecular Medicine, College of Medicine, University of South Florida, Tampa, Florida 33612, USA"},{"name":"H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, Florida 33612, USA"},{"name":"Department of Chemistry, University of South Florida, Tampa, Florida 33612, USA"}]}],"member":"219","published-online":{"date-parts":[[2012,4,8]]},"reference":[{"key":"rf1","unstructured":"H. A.\u00a0Dailey and T. A.\u00a0Dailey, The Porphyrin Handbook\u00a012, eds. K. M.\u00a0Kadish, K. M.\u00a0Smith and R.\u00a0Guilard (Elsevier Science, USA, 2003)\u00a0pp. 93\u2013121."},{"key":"rf2","doi-asserted-by":"publisher","DOI":"10.1007\/BF02110037"},{"key":"rf3","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2006.01.001"},{"key":"rf4","unstructured":"G. C.\u00a0Ferreira and G. A.\u00a0Hunter, The Handbook of Porphyrin Science\u00a015, eds. K. M.\u00a0Kadish, K. 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