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Enzymological and structural characterization of Arabidopsis thaliana heme oxygenase‐1

2022; Wiley; Volume: 12; Issue: 9 Linguagem: Inglês

10.1002/2211-5463.13453

2211-5463

Jia Wang, Xiaoyi Li, Jing‐Wen Chang, Tong Ye, Yingwei Mao, Xiao Wang, Lin Liu,

Cassava research and cyanide

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.