Crystal structure of higher plant heme oxygenase-1 and its mechanism of interaction with ferredoxin.
Amino Acid Sequence
Biliverdine
/ chemistry
Carbon Monoxide
/ chemistry
Catalytic Domain
Chloroplasts
/ chemistry
Cloning, Molecular
Crystallography, X-Ray
Escherichia coli
/ genetics
Ferredoxins
/ chemistry
Gene Expression
Genetic Vectors
/ chemistry
Heme
/ chemistry
Heme Oxygenase-1
/ chemistry
Hydrogen Bonding
Iron
/ chemistry
Molecular Docking Simulation
Nuclear Magnetic Resonance, Biomolecular
Plant Proteins
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Recombinant Proteins
/ chemistry
Sequence Alignment
Sequence Homology, Amino Acid
Glycine max
/ chemistry
Thylakoids
/ chemistry
ITC
NMR spectroscopy
X-ray crystallography
heme oxygenase
structural biology
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
Historique:
received:
08
10
2020
revised:
08
12
2020
accepted:
21
12
2020
pubmed:
12
4
2021
medline:
26
8
2021
entrez:
11
4
2021
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 33839679
pii: S0021-9258(20)00213-6
doi: 10.1074/jbc.RA120.016271
pmc: PMC7948506
pii:
doi:
Substances chimiques
Ferredoxins
0
Plant Proteins
0
Recombinant Proteins
0
Heme
42VZT0U6YR
Carbon Monoxide
7U1EE4V452
Iron
E1UOL152H7
Heme Oxygenase-1
EC 1.14.14.18
Biliverdine
O9MIA842K9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
100217Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
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