Heterologous expression and in vitro assembly of the transmembrane cytochrome b(6). Prodohl, A, Dreher, C, Hielscher, R, Hellwig, P, Schneider, D, Prodöhl, A, Dreher, C, Hielscher, R, Hellwig, P, Schneider, D, Prodohl, A, Dreher, C, Hielscher, R, Hellwig, P, Schneider, D, Prodöhl, A, Dreher, C, Hielscher, R, Hellwig, P, & Schneider, D Protein Expression and Purification, 56(2):279–285, 2007. ![Heterologous expression and in vitro assembly of the transmembrane cytochrome b(6) [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Folding and assembly studies with a-helical membrane proteins are often hampered by the absence of high-level expression systems as well as by missing suitable in vitro refolding procedures. Experimental constraints and requirements for heterologous expression and in vitro assembly of cytochrome b(6) have been examined and conditions for in vitro reconstitutions of the protein have been optimized. Cytochrome b6 can serve as an excellent model system for in vitro studies on the dynamic interplay of an apo-protein and heme cofactors during assembly of a transmembrane b-type cytochrome. In vitro assembled cytochrome b6 binds two hemes with different midpoint potentials and both ferri as well as ferro heme bind to the apo-cytochrome. However, the ferro cytochrome appears to be less stable than the ferri form. (C) 2007 Elsevier Inc. All rights reserved.
@article{prodohl_heterologous_2007,
title = {Heterologous expression and in vitro assembly of the transmembrane cytochrome b(6)},
volume = {56},
issn = {1046-5928 (Print) 1046-5928 (Linking)},
url = {http://www.ncbi.nlm.nih.gov/pubmed/17892950 http://www.sciencedirect.com/science/article/pii/S1046592807001957},
doi = {DOI 10.1016/j.pep.2007.08.007},
abstract = {Folding and assembly studies with a-helical membrane proteins are often hampered by the absence of high-level expression systems as well as by missing suitable in vitro refolding procedures. Experimental constraints and requirements for heterologous expression and in vitro assembly of cytochrome b(6) have been examined and conditions for in vitro reconstitutions of the protein have been optimized. Cytochrome b6 can serve as an excellent model system for in vitro studies on the dynamic interplay of an apo-protein and heme cofactors during assembly of a transmembrane b-type cytochrome. In vitro assembled cytochrome b6 binds two hemes with different midpoint potentials and both ferri as well as ferro heme bind to the apo-cytochrome. However, the ferro cytochrome appears to be less stable than the ferri form. (C) 2007 Elsevier Inc. All rights reserved.},
language = {English},
number = {2},
journal = {Protein Expression and Purification},
author = {Prodohl, A and Dreher, C and Hielscher, R and Hellwig, P and Schneider, D and Prodöhl, A and Dreher, C and Hielscher, R and Hellwig, P and Schneider, D and Prodohl, A and Dreher, C and Hielscher, R and Hellwig, P and Schneider, D and Prodöhl, A and Dreher, C and Hielscher, R and Hellwig, P and Schneider, D},
year = {2007},
pmid = {17892950},
keywords = {2-stage model, Cytochromes b6/*chemistry/genetics/*metabolism, Escherichia coli/genetics/metabolism, Membrane Proteins/chemistry/genetics/metabolism, Oxidation-Reduction, Plant Proteins/chemistry/genetics/metabolism, Protein Folding, assembly, b-type cytochrome, bacterial, complex, cytochrome b(6), escherichia-coli, heme, membrane-protein, midpoint potential, mixed micelles, spectroscopy, stability},
pages = {279--285},
}
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Experimental constraints and requirements for heterologous expression and in vitro assembly of cytochrome b(6) have been examined and conditions for in vitro reconstitutions of the protein have been optimized. Cytochrome b6 can serve as an excellent model system for in vitro studies on the dynamic interplay of an apo-protein and heme cofactors during assembly of a transmembrane b-type cytochrome. In vitro assembled cytochrome b6 binds two hemes with different midpoint potentials and both ferri as well as ferro heme bind to the apo-cytochrome. However, the ferro cytochrome appears to be less stable than the ferri form. (C) 2007 Elsevier Inc. All rights reserved.","language":"English","number":"2","journal":"Protein Expression and Purification","author":[{"propositions":[],"lastnames":["Prodohl"],"firstnames":["A"],"suffixes":[]},{"propositions":[],"lastnames":["Dreher"],"firstnames":["C"],"suffixes":[]},{"propositions":[],"lastnames":["Hielscher"],"firstnames":["R"],"suffixes":[]},{"propositions":[],"lastnames":["Hellwig"],"firstnames":["P"],"suffixes":[]},{"propositions":[],"lastnames":["Schneider"],"firstnames":["D"],"suffixes":[]},{"propositions":[],"lastnames":["Prodöhl"],"firstnames":["A"],"suffixes":[]},{"propositions":[],"lastnames":["Dreher"],"firstnames":["C"],"suffixes":[]},{"propositions":[],"lastnames":["Hielscher"],"firstnames":["R"],"suffixes":[]},{"propositions":[],"lastnames":["Hellwig"],"firstnames":["P"],"suffixes":[]},{"propositions":[],"lastnames":["Schneider"],"firstnames":["D"],"suffixes":[]},{"propositions":[],"lastnames":["Prodohl"],"firstnames":["A"],"suffixes":[]},{"propositions":[],"lastnames":["Dreher"],"firstnames":["C"],"suffixes":[]},{"propositions":[],"lastnames":["Hielscher"],"firstnames":["R"],"suffixes":[]},{"propositions":[],"lastnames":["Hellwig"],"firstnames":["P"],"suffixes":[]},{"propositions":[],"lastnames":["Schneider"],"firstnames":["D"],"suffixes":[]},{"propositions":[],"lastnames":["Prodöhl"],"firstnames":["A"],"suffixes":[]},{"propositions":[],"lastnames":["Dreher"],"firstnames":["C"],"suffixes":[]},{"propositions":[],"lastnames":["Hielscher"],"firstnames":["R"],"suffixes":[]},{"propositions":[],"lastnames":["Hellwig"],"firstnames":["P"],"suffixes":[]},{"propositions":[],"lastnames":["Schneider"],"firstnames":["D"],"suffixes":[]}],"year":"2007","pmid":"17892950","keywords":"2-stage model, Cytochromes b6/*chemistry/genetics/*metabolism, Escherichia coli/genetics/metabolism, Membrane Proteins/chemistry/genetics/metabolism, Oxidation-Reduction, Plant Proteins/chemistry/genetics/metabolism, Protein Folding, assembly, b-type cytochrome, bacterial, complex, cytochrome b(6), escherichia-coli, heme, membrane-protein, midpoint potential, mixed micelles, spectroscopy, stability","pages":"279–285","bibtex":"@article{prodohl_heterologous_2007,\n\ttitle = {Heterologous expression and in vitro assembly of the transmembrane cytochrome b(6)},\n\tvolume = {56},\n\tissn = {1046-5928 (Print) 1046-5928 (Linking)},\n\turl = {http://www.ncbi.nlm.nih.gov/pubmed/17892950 http://www.sciencedirect.com/science/article/pii/S1046592807001957},\n\tdoi = {DOI 10.1016/j.pep.2007.08.007},\n\tabstract = {Folding and assembly studies with a-helical membrane proteins are often hampered by the absence of high-level expression systems as well as by missing suitable in vitro refolding procedures. Experimental constraints and requirements for heterologous expression and in vitro assembly of cytochrome b(6) have been examined and conditions for in vitro reconstitutions of the protein have been optimized. Cytochrome b6 can serve as an excellent model system for in vitro studies on the dynamic interplay of an apo-protein and heme cofactors during assembly of a transmembrane b-type cytochrome. In vitro assembled cytochrome b6 binds two hemes with different midpoint potentials and both ferri as well as ferro heme bind to the apo-cytochrome. However, the ferro cytochrome appears to be less stable than the ferri form. (C) 2007 Elsevier Inc. 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