Open AccessEnzymological and structural characterization of Arabidopsis thaliana heme oxygenase‐1
Author(s) -
Wang Jia,
Li Xiaoyi,
Chang JingWen,
Ye Tong,
Mao Ying,
Wang Xiao,
Liu Lin
Publication year - 2022
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.13453
Subject(s) - heme , ferredoxin , arabidopsis thaliana , oxygenase , heme oxygenase , biochemistry , enzyme , arabidopsis , chemistry , oxidoreductase , reductase , biology , mutant , gene
Arabidopsis thaliana heme oxygenase‐1 (AtHO‐1), a metabolic enzyme in the heme degradation pathway, serves as a prototype for study of the bilin‐related functions in plants. Past biological analyses revealed that AtHO‐1 requires ferredoxin‐NADP + reductase (FNR) and ferredoxin for its enzymatic activity. Here, we characterized the binding and degradation of heme by AtHO‐1, and found that ferredoxin is a dispensable component of the reducing system that provides electrons for heme oxidation. Furthermore, we reported the crystal structure of heme‐bound AtHO‐1, which demonstrates both conserved and previously undescribed features of plant heme oxygenases. Finally, the electron transfer pathway from FNR to AtHO‐1 is suggested based on the known structural information.