ArticleFEBS letters2016
The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.
Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The structural chemistry and biosynthesis of chlorophylls.RSC chemical biology · 2026Review
- Metals in Motion: Understanding Labile Metal Pools in Bacteria.Biochemistry · 2025Review
- Mutagenesis selection and large-scale cultivation of non-greenFrontiers in nutrition · 2024Article
- Chlorophyll biosynthesis under the control of arginine metabolism.Cell reports · 2023Article
- The active site of magnesium chelatase.Nature plants · 2020Article
- Heterologous Expression of the Barley (Hordeum vulgare L.) Xantha-f, -g and -h Genes that Encode Magnesium Chelatase Subunits.The protein journal · 2020Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- Hexameric structure of the ATPase motor subunit of magnesium chelatase in chlorophyll biosynthesis.Protein science : a publication of the Protein Society · 2020Article
- A Photosynthesis-Specific Rubredoxin-Like Protein Is Required for Efficient Association of the D1 and D2 Proteins during the Initial Steps of Photosystem II Assembly.The Plant cell · 2019Article
- The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase.The Biochemical journal · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
In the first committed reaction of chlorophyll biosynthesis, magnesium chelatase couples ATP hydrolysis to the thermodynamically unfavorable Mg(2+) insertion into protoporphyrin IX (ΔG°' of circa 25-33 kJ·mol(-1) ). We explored the thermodynamic constraints on magnesium chelatase and demonstrate the effect of nucleotide hydrolysis on both the reaction kinetics and thermodynamics. The enzyme produces a significant rate enhancement (kcat /kuncat of 400 × 10(6) m) and a catalytic rate enhancement, kcat/KmDIXK0.5Mgkuncat, of 30 × 10(15) m(-1) , increasing to 300 × 10(15) m(-1) with the activator protein Gun4. This is the first demonstration of the thermodynamic benefit of ATP hydrolysis in the AAA(+) family.
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