title: In vitro evaluation of mitochondrial-chloroplast subcellular localization of heme oxygenase1 (HO1) in Glycine max.
abstract: Heme oxygenase1 (HO1) catalyzes the degradation of heme in to biliverdin, carbon monoxide, and ferrous ions. Its role in higher plants has been found as an antioxidant and precursor of phytochrome synthesis. The present study focuses on subcellular localization of HO1 in leaves of soybean has been investigated. Most activity appeared to be located within chloroplast due to its role in phytochrome synthesis but mitochondria also share its localization. Mitochondrial location of HO1 might be on its inner membranous space due to its role in the synthesis of electron donor species which facilitates HO1 catalyzed reaction. Study reports the co-localization of HO1 in both chloroplast and mitochondria.
authors.affiliation: Department of Bioscience and Biotechnology, Banasthali University, Banasthali, 304022, India.
authors.forename: Shubham
authors.initials: S
authors.lastname: Dixit
authors.forename: Khushbu
authors.initials: K
authors.lastname: Verma
authors.forename: Gyan Singh
authors.initials: GS
authors.lastname: Shekhawat
mesh_terms: D002736:Chloroplasts / Q000378:metabolism*; D051547:Heme Oxygenase-1 / Q000378:metabolism*; D008928:Mitochondria / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D013025:Glycine max / Q000201:enzymology*
chemical_list: D010940:Plant Proteins; D051547:Heme Oxygenase-1