ArticleMolecular microbiology2014
Identification and characterization of the 'missing' terminal enzyme for siroheme biosynthesis in α-proteobacteria.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Structural insights into the recognition of tetrapyrrole substrates by ancestral class II chelatase CfbA.Protein science : a publication of the Protein Society · 2024Article
- The nickel-sirohydrochlorin formation mechanism of the ancestral class II chelatase CfbA in coenzyme F430 biosynthesis.Chemical science · 2021Article
- The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021Review
- Optimization of hydrogenobyrinic acid biosynthesis in Escherichia coli using multi-level metabolic engineering strategies.Microbial cell factories · 2020Article
- Biosynthesis of the modified tetrapyrroles-the pigments of life.The Journal of biological chemistry · 2020Review
- Adaptation to Photooxidative Stress: Common and Special Strategies of the AlphaproteobacteriaMicroorganisms · 2020Article
- Identifying term relations cross different gene ontology categories.BMC bioinformatics · 2017Article
- Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Microbiology and molecular biology reviews : MMBR · 2017Review
- Reactions of Ferrous Coproheme Decarboxylase (HemQ) with OBiochemistry · 2017Article
- Transfer and Persistence of a Multi-Drug Resistance PlasmidFrontiers in microbiology · 2017Article
- The structure, function and properties of sirohaem decarboxylase--an enzyme with structural homology to a transcription factor family that is part of the alternative haem biosynthesis pathway.Molecular microbiology · 2014Article
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Authors and funding
7 authors.
Funding
Abstract
It has recently been shown that the biosynthetic route for both the d1 -haem cofactor of dissimilatory cd1 nitrite reductases and haem, via the novel alternative-haem-synthesis pathway, involves siroheme as an intermediate, which was previously thought to occur only as a cofactor in assimilatory sulphite/nitrite reductases. In many denitrifiers (which require d1 -haem), the pathway to make siroheme remained to be identified. Here we identify and characterize a sirohydrochlorin-ferrochelatase from Paracoccus pantotrophus that catalyses the last step of siroheme synthesis. It is encoded by a gene annotated as cbiX that was previously assumed to be encoding a cobaltochelatase, acting on sirohydrochlorin. Expressing this chelatase from a plasmid restored the wild-type phenotype of an Escherichia coli mutant-strain lacking sirohydrochlorin-ferrochelatase activity, showing that this chelatase can act in the in vivo siroheme synthesis. A ΔcbiX mutant in P. denitrificans was unable to respire anaerobically on nitrate, proving the role of siroheme as a precursor to another cofactor. We report the 1.9 Å crystal structure of this ferrochelatase. In vivo analysis of single amino acid variants of this chelatase suggests that two histidines, His127 and His187, are essential for siroheme synthesis. This CbiX can generally be identified in α-proteobacteria as the terminal enzyme of siroheme biosynthesis.
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