ArticleThe Journal of biological chemistry2016
Crystal Structure and Catalytic Mechanism of 7-Hydroxymethyl Chlorophyll a Reductase.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- ChlorophyllPlants (Basel, Switzerland) · 2026Article
- Structural Characterization of the Chlorophyllide a Oxygenase (CAO) Enzyme Through an In Silico Approach.Journal of molecular evolution · 2023Article
- Physiological and transcriptomic analyses provide insight into thermotolerance in desert plant Zygophyllum xanthoxylum.BMC plant biology · 2023Article
- Rieske Oxygenase Catalyzed C-H Bond Functionalization Reactions in ChlorophyllACS central science · 2022Article
- Enzymological and structural characterization of Arabidopsis thaliana heme oxygenase-1.FEBS open bio · 2022Article
- Overexpression of 7-hydroxymethyl ChlorophyllPlants (Basel, Switzerland) · 2021Article
- Insights into the structure and function of the rate-limiting enzyme of chlorophyll degradation through analysis of a bacterial Mg-dechelatase homolog.Computational and structural biotechnology journal · 2021Article
- A Synthetic Cytokinin Improves Photosynthesis in Rice under Drought Stress by Modulating the Abundance of Proteins Related to Stomatal Conductance, Chlorophyll Contents, and Rubisco Activity.Plants (Basel, Switzerland) · 2020Article
- Structural basis for plant lutein biosynthesis from α-carotene.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Rice 7-Hydroxymethyl ChlorophyllMolecules and cells · 2017Article
- The iron-sulfur cluster biosynthesis protein SUFB is required for chlorophyll synthesis, but not phytochrome signaling.The Plant journal : for cell and molecular biology · 2017Article
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
7-Hydroxymethyl chlorophyll a reductase (HCAR) catalyzes the second half-reaction in chlorophyll b to chlorophyll a conversion. HCAR is required for the degradation of light-harvesting complexes and is necessary for efficient photosynthesis by balancing the chlorophyll a/b ratio. Reduction of the hydroxymethyl group uses redox cofactors [4Fe-4S] cluster and FAD to transfer electrons and is difficult because of the strong carbon-oxygen bond. Here, we report the crystal structure of Arabidopsis HCAR at 2.7-Å resolution and reveal that two [4Fe-4S]clusters and one FAD within a very short distance form a consecutive electron pathway to the substrate pocket. In vitro kinetic analysis confirms the ferredoxin-dependent electron transport chain, thus supporting a proton-activated electron transfer mechanism. HCAR resembles a partial reconstruction of an archaeal F420-reducing [NiFe] hydrogenase, which suggests a common mode of efficient proton-coupled electron transfer through conserved cofactor arrangements. Furthermore, the trimeric form of HCAR provides a biological clue of its interaction with light-harvesting complex II.
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