ArticleProceedings of the National Academy of Sciences of the United States of America2004
Biosynthesis of artificial microperoxidases by exploiting the secretion and cytochrome c maturation apparatuses of Escherichia coli.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 51 citations in OpenAlex.
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Symmetry-related residues as promising hotspots for the evolution ofChemical science · 2021Article
- Reductive nitrosylation of ferric microperoxidase-11.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Influence of heme c attachment on heme conformation and potential.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Totally synthetic microperoxidase-11.Royal Society open science · 2018Article
- Structure and Catalysis of Fe(III) and Cu(II) Microperoxidase-11 Interacting with the Positively Charged Interfaces of Lipids.Molecules (Basel, Switzerland) · 2017Article
- 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
- Nanostructures for peroxidases.Frontiers in molecular biosciences · 2015Review
- Introduction of a covalent histidine-heme linkage in a hemoglobin: a promising tool for heme protein engineering.Journal of inorganic biochemistry · 2014Article
- Constructing a man-made c-type cytochrome maquetteChemical science · 2014Article
- In vitro and cellular self-assembly of a Zn-binding protein cryptand via templated disulfide bonds.Journal of the American Chemical Society · 2013Article
- Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.Scientifica · 2013Review
- Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.Biochimica et biophysica acta · 2012Article
- Cytochrome c biogenesis System I.The FEBS journal · 2011Review
- Comparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis.Metallomics : integrated biometal science · 2011Article
- Modular and versatile hybrid coordination motifs on alpha-helical protein surfaces.Inorganic chemistry · 2010Article
- Evolution of metal selectivity in templated protein interfaces.Journal of the American Chemical Society · 2010Article
- Controlled protein dimerization through hybrid coordination motifs.Inorganic chemistry · 2010Article
- Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control.Microbiology and molecular biology reviews : MMBR · 2009Review
- The chemistry and biochemistry of heme c: functional bases for covalent attachment.Natural product reports · 2008Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microperoxidases were initially isolated as peptide fragments containing covalently bound heme and are derived from naturally occurring c-type cytochromes. They are not only used as model compounds but also have potential applications as biosensors, electron carriers, photoreceptors, microzymes, and drugs. In a systematic attempt to define the minimal requirements for covalent attachment of hemes to c-type cytochromes, we have succeeded to produce artificial microperoxidases with peptide sequences that do not occur naturally and can be manipulated. The in vivo production of these microperoxidases requires targeting of the peptide to the bacterial periplasm, proteolytic processing of the signal peptide, and covalent attachment of heme to the signature motif CXXCH by the cytochrome c maturation proteins CcmA-H. The peptides that bind heme carry a C-terminal histidine tag, presumably to stabilize the heme peptide. We present a heme cassette that is the basis for the de novo design of functional hemoproteins.
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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.