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Research Article

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

A F Wagner, M Frey, F A Neugebauer, W Schäfer, and J Knappe
PNAS February 1, 1992 89 (3) 996-1000; https://doi.org/10.1073/pnas.89.3.996
A F Wagner
Institut für Biologische Chemie, Universität Heidelberg, Federal Republic of Germany.
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M Frey
Institut für Biologische Chemie, Universität Heidelberg, Federal Republic of Germany.
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F A Neugebauer
Institut für Biologische Chemie, Universität Heidelberg, Federal Republic of Germany.
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W Schäfer
Institut für Biologische Chemie, Universität Heidelberg, Federal Republic of Germany.
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J Knappe
Institut für Biologische Chemie, Universität Heidelberg, Federal Republic of Germany.
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Abstract

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

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The free radical in pyruvate formate-lyase is located on glycine-734.
A F Wagner, M Frey, F A Neugebauer, W Schäfer, J Knappe
Proceedings of the National Academy of Sciences Feb 1992, 89 (3) 996-1000; DOI: 10.1073/pnas.89.3.996
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Proceedings of the National Academy of Sciences: 116 (49)
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