ArticleBiochimica et biophysica acta2012
Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.
Article in Biochimica et biophysica acta, 2012. 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, 16 citations in OpenAlex.
- 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
- Structural basis of membrane machines that traffick and attach heme to cytochromes.The Journal of biological chemistry · 2023Article
- Cysteine Redox Chemistry in Peptide Self-Assembly to Modulate Hydrogelation.Molecules (Basel, Switzerland) · 2023Article
- Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport.Nature chemical biology · 2022Article
- Maturation of PlastidFrontiers in plant science · 2017Review
- Molecular Basis Behind Inability of Mitochondrial Holocytochrome c Synthase to Mature Bacterial Cytochromes: DEFINING A CRITICAL ROLE FOR CYTOCHROME c α HELIX-1.The Journal of biological chemistry · 2016Article
- Cytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Biochimica et biophysica acta · 2014Review
- The CcmFH complex is the system I holocytochrome c synthetase: engineering cytochrome c maturation independent of CcmABCDE.Molecular microbiology · 2014Article
- 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
- Engineering a prokaryotic apocytochrome c as an efficient substrate for Saccharomyces cerevisiae cytochrome c heme lyase.Biochemical and biophysical research communications · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The reconstitution of biosynthetic pathways from heterologous hosts can help define the minimal genetic requirements for pathway function and facilitate detailed mechanistic studies. Each of the three pathways for the assembly of cytochrome c in nature (called systems I, II, and III) has been shown to function recombinantly in Escherichia coli, covalently attaching heme to the cysteine residues of a CXXCH motif of a c-type cytochrome. However, recombinant systems I (CcmABCDEFGH) and II (CcsBA) function in the E. coli periplasm, while recombinant system III (CCHL) attaches heme to its cognate receptor in the cytoplasm of E. coli, which makes direct comparisons between the three systems difficult. Here we show that the human CCHL (with a secretion signal) attaches heme to the human cytochrome c (with a signal sequence) in the E. coli periplasm, which is bioenergetically (p-side) analogous to the mitochondrial intermembrane space. The human CCHL is specific for the human cytochrome c, whereas recombinant system II can attach heme to multiple non-cognate c-type cytochromes (possessing the CXXCH motif.) We also show that the recombinant periplasmic systems II and III use components of the natural E. coli periplasmic DsbC/DsbD thiol-reduction pathway. This article is part of a Special Issue entitled: Biogenesis/Assembly of Respiratory Enzyme Complexes.
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