ArticlePlant physiology2011
Functional assignments for the carboxyl-terminal domains of the ferrochelatase from Synechocystis PCC 6803: the CAB domain plays a regulatory role, and region II is essential for catalysis.
Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 45 citations in OpenAlex.
- Milestones in the Elucidation of Heme Biosynthesis.Chemical reviews · 2026Review
- Localization of heme biosynthesis in the diatomFrontiers in plant science · 2025Article
- Leaf Color Classification and Expression Analysis of Photosynthesis-Related Genes in Inbred Lines of Chinese Cabbage Displaying Minor Variations in Dark-Green Leaves.Plants (Basel, Switzerland) · 2023Article
- Retrograde signaling in plants: A critical review focusing on the GUN pathway and beyond.Plant communications · 2023Review
- Using Diatom and Apicomplexan Models to Study the Heme Pathway ofInternational journal of molecular sciences · 2021Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- ONE-HELIX PROTEIN1 and 2 Form Heterodimers to Bind Chlorophyll in Photosystem II Biogenesis.Plant physiology · 2020Article
- A lil3 chlp double mutant with exclusive accumulation of geranylgeranyl chlorophyll displays a lethal phenotype in rice.BMC plant biology · 2019Article
- The antenna-like domain of the cyanobacterial ferrochelatase can bind chlorophyll and carotenoids in an energy-dissipative configuration.The Journal of biological chemistry · 2019Article
- The stress-induced SCP/HLIP family of small light-harvesting-like proteins (ScpABCDE) protects Photosystem II from photoinhibitory damages in the cyanobacterium Synechocystis sp. PCC 6803.Photosynthesis research · 2018Article
- Complete enzyme set for chlorophyll biosynthesis inScience advances · 2018Article
- PufQ regulates porphyrin flux at the haem/bacteriochlorophyll branchpoint of tetrapyrrole biosynthesis via interactions with ferrochelatase.Molecular microbiology · 2017Article
- Salt stress-induced FERROCHELATASE 1 improves resistance to salt stress by limiting sodium accumulation in Arabidopsis thaliana.Scientific reports · 2017Article
- LIL3, a Light-Harvesting Complex Protein, Links Terpenoid and Tetrapyrrole Biosynthesis inPlant physiology · 2017Article
- Conserved residues in Ycf54 are required for protochlorophyllide formation inThe Biochemical journal · 2017Article
- Allocation of Heme Is Differentially Regulated by Ferrochelatase Isoforms in Arabidopsis Cells.Frontiers in plant science · 2016Article
- Synthesis of Chlorophyll-Binding Proteins in a Fully Segregated Δycf54 Strain of the Cyanobacterium Synechocystis PCC 6803.Frontiers in plant science · 2016Article
- Organization of chlorophyll biosynthesis and insertion of chlorophyll into the chlorophyll-binding proteins in chloroplasts.Photosynthesis research · 2015Review
- A cyanobacterial chlorophyll synthase-HliD complex associates with the Ycf39 protein and the YidC/Alb3 insertase.The Plant cell · 2014Article
- Making proteins green; biosynthesis of chlorophyll-binding proteins in cyanobacteria.Photosynthesis research · 2014Review
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
Abstract
Ferrochelatase (FeCH) catalyzes the insertion of Fe(2+) into protoporphyrin, forming protoheme. In photosynthetic organisms, FeCH and magnesium chelatase lie at a biosynthetic branch point where partitioning down the heme and chlorophyll (Chl) pathways occurs. Unlike their mammalian, yeast, and other bacterial counterparts, cyanobacterial and algal FeCHs as well as FeCH2 isoform from plants possess a carboxyl-terminal Chl a/b-binding (CAB) domain with a conserved Chl-binding motif. The CAB domain is connected to the FeCH catalytic core by a proline-rich linker sequence (region II). In order to dissect the regulatory, catalytic, and structural roles of the region II and CAB domains, we analyzed a FeCH ΔH347 mutant that retains region II but lacks the CAB domain and compared it with the ΔH324-FeCH mutant that lacks both these domains. We found that the CAB domain is not required for catalytic activity but is essential for dimerization of FeCH; its absence causes aberrant accumulation of Chl-protein complexes under high light accompanied by high levels of the Chl precursor chlorophyllide. Thus, the CAB domain appears to serve mainly a regulatory function, possibly in balancing Chl biosynthesis with the synthesis of cognate apoproteins. Region II is essential for the catalytic function of the plastid-type FeCH enzyme, although the low residual activity of the ΔH324-FeCH is more than sufficient to furnish the cellular demand for heme. We propose that the apparent surplus of FeCH activity in the wild type is critical for cell viability under high light due to a regulatory role of FeCH in the distribution of Chl into apoproteins.
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