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  The free radical in pyruvate formate-lyase is located on glycine-734

Wagner, A. F. V., Frey, M., Neugebauer, F. A., Schäfer, W., & Knappe, J. (1992). The free radical in pyruvate formate-lyase is located on glycine-734. Proceedings of the National Academy of Sciences of the United States of America, 89(3), 996-1000. doi:10.1073/pnas.89.3.996.

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Datensatz-Permalink: https://hdl.handle.net/11858/00-001M-0000-002B-080C-1 Versions-Permalink: https://hdl.handle.net/21.11116/0000-0002-5924-2
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PNAS_89_1992_996.pdf (beliebiger Volltext), 2MB
 
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 Urheber:
Wagner, A. F. Volker, Autor
Frey, Manfred, Autor
Neugebauer, Franz A.1, Autor           
Schäfer, Wolfram, Autor
Knappe, Joachim, Autor
Affiliations:
1Department of Organic Chemistry, Max Planck Institute for Medical Research, Max Planck Society, ou_1497706              

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 Zusammenfassung: Pyruvate formate-lyase (acetyl-CoA:formate C-acetyltransferase, EC 2.3.1.54) from anaerobic Escherichia coli cells converts pyruvate to acetyl-CoA and formate by a unique homolytic mechanism that involves a free radical harbored in the protein structure. By EPR spectroscopy of selectively 13C-labeled enzyme, the radical (g = 2.0037) has been assigned to carbon-2 of a glycine residue. Estimated hyperfine coupling constants to the central 13C nucleus (A parallel = 4.9 mT and A perpendicular = 0.1 mT) and to 13C nuclei in alpha and beta positions agree with literature data for glycine radical models. N-coupling was verified through uniform 15N-labeling. The large 1H hyperfine splitting (1.5 mT) dominating the EPR spectrum was assigned to the alpha proton, which in the enzyme radical is readily solvent-exchangeable. Oxygen destruction of the radical produced two unique fragments (82 and 3 kDa) of the constituent polypeptide chain. The N-terminal block on the small fragment was identified by mass spectrometry as an oxalyl residue that derives from Gly-734, thus assigning the primary structural glycyl radical position. The carbon-centered radical is probably resonance-stabilized through the adjacent carboxamide groups in the polypeptide main chain and could be comparable energetically with other known protein radicals carrying the unpaired electron in tyrosine or tryptophan residues.

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Sprache(n): eng - English
 Datum: 1991-08-221991-10-231992-02-01
 Publikationsstatus: Erschienen
 Seiten: 5
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1073/pnas.89.3.996
URI: https://www.ncbi.nlm.nih.gov/pubmed/1310545
URI: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC48372/
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Titel: Proceedings of the National Academy of Sciences of the United States of America
  Andere : Proc. Acad. Sci. USA
  Andere : Proc. Acad. Sci. U.S.A.
  Andere : Proceedings of the National Academy of Sciences of the USA
  Kurztitel : PNAS
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Washington, D.C. : National Academy of Sciences
Seiten: - Band / Heft: 89 (3) Artikelnummer: - Start- / Endseite: 996 - 1000 Identifikator: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230