ArticleProtein science : a publication of the Protein Society2000
Integrity of thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: biochemical, spectral, and structural characterization of the recombinant protein.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 48 citations in OpenAlex.
- Insertion of the FeFEBS letters · 2025Article
- An engineered thermally tolerant apo-cytochrome scaffold for metal-less incorporation of heme derivative.PloS one · 2023Article
- Investigations of the low-frequency spectral density of cytochrome c upon equilibrium unfolding.The journal of physical chemistry. B · 2013Article
- Characterization of the nitric oxide reductase from Thermus thermophilus.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Snapshots of a protein folding intermediate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modulation of ligand-field parameters by heme ruffling in cytochromes c revealed by EPR spectroscopy.Inorganic chemistry · 2011Article
- Comparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis.Metallomics : integrated biometal science · 2011Article
- A heme fusion tag for protein affinity purification and quantification.Protein science : a publication of the Protein Society · 2010Article
- The diheme cytochrome c(4) from Vibrio cholerae is a natural electron donor to the respiratory cbb(3) oxygen reductase.Biochemistry · 2010Article
- Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba3 Cytochrome c oxidase from Thermus thermophilus.Biochemistry · 2010Article
- NMR and DFT investigation of heme ruffling: functional implications for cytochrome c.Journal of the American Chemical Society · 2010Article
- Overexpression, characterization, and crystallization of the functional domain of cytochrome c(z) from Chlorobium tepidum.Photosynthesis research · 2009Article
- The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- The chemistry and biochemistry of heme c: functional bases for covalent attachment.Natural product reports · 2008Review
- Toward a chemical mechanism of proton pumping by the B-type cytochrome c oxidases: application of density functional theory to cytochrome ba3 of Thermus thermophilus.Journal of the American Chemical Society · 2008Article
- Native and unfolded cytochrome c--comparison of dynamics using 2D-IR vibrational echo spectroscopy.The journal of physical chemistry. B · 2008Article
- The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystallography.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2006Review
- C-type cytochromes: diverse structures and biogenesis systems pose evolutionary problems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003Review
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14 authors at 6 institutions in 2 countries.
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Abstract
We describe the design of Escherichia coli cells that synthesize a structurally perfect, recombinant cytochrome c from the Thermus thermophilus cytochrome c552 gene. Key features are (1) construction of a plasmid-borne, chimeric cycA gene encoding an Escherichia coli-compatible, N-terminal signal sequence (MetLysIleSerIleTyrAlaThrLeu AlaAlaLeuSerLeuAlaLeuProAlaGlyAla) followed by the amino acid sequence of mature Thermus cytochrome c552; and (2) coexpression of the chimeric cycA gene with plasmid-borne, host-specific cytochrome c maturation genes (ccmABCDEFGH). Approximately 1 mg of purified protein is obtained from 1 L of culture medium. The recombinant protein, cytochrome rsC552, and native cytochrome c552 have identical redox potentials and are equally active as electron transfer substrates toward cytochrome ba3, a Thermus heme-copper oxidase. Native and recombinant cytochromes c were compared and found to be identical using circular dichroism, optical absorption, resonance Raman, and 500 MHz 1H-NMR spectroscopies. The 1.7 A resolution X-ray crystallographic structure of the recombinant protein was determined and is indistinguishable from that reported for the native protein (Than, ME, Hof P, Huber R, Bourenkov GP, Bartunik HD, Buse G, Soulimane T, 1997, J Mol Biol 271:629-644). This approach may be generally useful for expression of alien cytochrome c genes in E. coli.
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