ArticleJournal of bacteriology2007
Heme concentration dependence and metalloporphyrin inhibition of the system I and II cytochrome c assembly pathways.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed.
- Towards Bacterial Resistance via the Membrane Strategy: Enzymatic, Biophysical and Biomimetic Studies of the Lipid cis-trans Isomerase of Pseudomonas aeruginosa.Chembiochem : a European journal of chemical biology · 2025Article
- Helicobacter pylori and Campylobacter jejuni bacterial holocytochrome c synthase structure-function analysis reveals conservation of heme binding.Communications biology · 2024Article
- Recombinant Biogenesis and Analysis of Cytochrome c Species.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Structures of the CcmABCD heme release complex at multiple states.Nature communications · 2022Article
- In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases.eLife · 2021Article
- Article
- Noble-Metal Substitution in Hemoproteins: An Emerging Strategy for Abiological Catalysis.Accounts of chemical research · 2019Article
- Comparative genomics sheds light on niche differentiation and the evolutionary history of comammox Nitrospira.The ISME journal · 2018Article
- Regulation of intracellular heme trafficking revealed by subcellular reporters.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins.Biochemistry · 2016Article
- Mitochondrial cytochrome c biogenesis: no longer an enigma.Trends in biochemical sciences · 2015Review
- The CcmFH complex is the system I holocytochrome c synthetase: engineering cytochrome c maturation independent of CcmABCDE.Molecular microbiology · 2014Article
- Interaction of holoCcmE with CcmF in heme trafficking and cytochrome c biosynthesis.Journal of molecular biology · 2014Article
- Development of recombinant hemoglobin-based oxygen carriers.Antioxidants & redox signaling · 2013Review
- Human mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome c.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.Biochimica et biophysica acta · 2012Article
- Heme ligand identification and redox properties of the cytochrome c synthetase, CcmF.Biochemistry · 2011Article
- Metal-substituted protein MRI contrast agents engineered for enhanced relaxivity and ligand sensitivity.Journal of the American Chemical Society · 2011Article
- Essential histidine pairs indicate conserved haem binding in epsilonproteobacterial cytochrome c haem lyases.Microbiology (Reading, England) · 2010Article
- The CcmC:heme:CcmE complex in heme trafficking and cytochrome c biosynthesis.Journal of molecular biology · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Studies have indicated that specific heme delivery to apocytochrome c is a critical feature of the cytochrome c biogenesis pathways called system I and II. To determine directly the heme requirements of each system, including whether other metal porphyrins can be incorporated into cytochromes c, we engineered Escherichia coli so that the natural system I (ccmABCDEFGH) was deleted and exogenous porphyrins were the sole source of porphyrins (Delta hemA). The engineered E. coli strains that produced recombinant system I (from E. coli) or system II (from Helicobacter) facilitated studies of the heme concentration dependence of each system. Using this exogenous porphyrin approach, it was shown that in system I the levels of heme used are at least fivefold lower than the levels used in system II, providing an important advantage for system I. Neither system could assemble holocytochromes c with other metal porphyrins, suggesting that the attachment mechanism is specific for Fe protoporphyrin. Surprisingly, Zn and Sn protoporphyrins are potent inhibitors of the pathways, and exogenous heme competes with this inhibition. We propose that the targets are the heme binding proteins in the pathways (CcmC, CcmE, and CcmF for system I and CcsA for system II).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.