Identification of the Mitochondrial Heme Metabolism Complex

• DOI: 10.1371/journal.pone.0135896
• Publication Date: 2015-08-19T18:02:28Z
• Authors: Amy E. Medlock; Mesafint T. Shiferaw; Jason R. Marcero; Ajay A. Vashisht; James A. Wohlschl...; John D. Phillips; Harry A. Dailey
• Keywords: Ferrochelatase; Protoporphyrinogen oxidase; Hemeprotein; Immunoprecipitation; Heme A

Heme is an essential cofactor for most organisms and all metazoans. While the individual enzymes involved in synthesis utilization of heme are fairly well known, less known about intracellular trafficking porphyrins heme, or regulation biosynthesis via protein complexes. To better understand this process we have undertaken a study macromolecular assemblies associated with synthesis. Herein utilized mass spectrometry coimmunoprecipitation tagged biosynthetic pathway developing erythroid cell culture model to identify putative partners. The validity these data obtained system confirmed by normal porphyrin/heme production engineered cells. Data consistent presence mitochondrial metabolism complex which minimally consists ferrochelatase, protoporphyrinogen oxidase aminolevulinic acid synthase-2. Additional proteins iron intermediary as transporters were identified potential partners complex. location components support transient protein-protein interactions within dynamic