Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin
| Autor: | Catharina T. Migita, Xuhong Zhang, Genji Kurisu, Takahisa Ikegami, Hideaki Tanaka, Rei Tohda, Tsuyoshi Konuma, Risa Mutoh, Young-Ho Lee |
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| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Protein Conformation alpha-Helical Chloroplasts Gene Expression Crystallography X-Ray Biochemistry Thylakoids rHO-1 rat HO isozyme1 chemistry.chemical_compound DSC differential scanning calorimetry Fe–SAD iron single-wavelength anomalous dispersion Catalytic Domain structural biology Cloning Molecular Heme Ferredoxin Plant Proteins Carbon Monoxide food and beverages Cytochrome P450 reductase Nuclear magnetic resonance spectroscopy heme oxygenase Recombinant Proteins Molecular Docking Simulation CO carbon monoxide Thylakoid Ferredoxins Research Article Protein Binding SynHO-1 Synechocystis sp PCC6803. isozyme1 Stereochemistry Iron Genetic Vectors FNR Fd–NADP+ reductase 03 medical and health sciences NMR spectroscopy Escherichia coli HO heme oxygenase Protein Interaction Domains and Motifs Amino Acid Sequence CPR cytochrome P450 reductase Molecular Biology Nuclear Magnetic Resonance Biomolecular X-ray crystallography Biliverdin 030102 biochemistry & molecular biology Sequence Homology Amino Acid Fd ferredoxin Biliverdine GmHO-1 Glycine max (soybean) HO-1 Isothermal titration calorimetry Hydrogen Bonding Cell Biology ITC Heme oxygenase hHO-1 human HO isozyme1 030104 developmental biology chemistry Protein Conformation beta-Strand Soybeans Sequence Alignment Heme Oxygenase-1 |
| Zdroj: | The Journal of Biological Chemistry |
| ISSN: | 1083-351X |
| Popis: | Heme oxygenase (HO) converts heme to carbon monoxide, biliverdin, and free iron, products that are essential in cellular redox signaling and iron recycling. In higher plants, HO is also involved in the biosynthesis of photoreceptor pigment precursors. Despite many common enzymatic reactions, the amino acid sequence identity between plant-type and other HOs is exceptionally low (∼19.5%), and amino acids that are catalytically important in mammalian HO are not conserved in plant-type HOs. Structural characterization of plant-type HO is limited to spectroscopic characterization by electron spin resonance, and it remains unclear how the structure of plant-type HO differs from that of other HOs. Here, we have solved the crystal structure of Glycine max (soybean) HO-1 (GmHO-1) at a resolution of 1.06 Å and carried out the isothermal titration calorimetry measurements and NMR spectroscopic studies of its interaction with ferredoxin, the plant-specific electron donor. The high-resolution X-ray structure of GmHO-1 reveals several novel structural components: an additional irregularly structured region, a new water tunnel from the active site to the surface, and a hydrogen-bonding network unique to plant-type HOs. Structurally important features in other HOs, such as His ligation to the bound heme, are conserved in GmHO-1. Based on combined data from X-ray crystallography, isothermal titration calorimetry, and NMR measurements, we propose the evolutionary fine-tuning of plant-type HOs for ferredoxin dependency in order to allow adaptation to dynamic pH changes on the stroma side of the thylakoid membrane in chloroplast without losing enzymatic activity under conditions of fluctuating light. |
| Databáze: | OpenAIRE |
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