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Fig. 3 EPR and ENDOR spectra of isotope-labeled intermediates and crystal structures of SAM-bound CmnDph2. EPR and ENDOR spectra of isotope-labeled intermediates.

Published byIrma Szilágyiné Modified over 5 years ago

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Presentation on theme: "Fig. 3 EPR and ENDOR spectra of isotope-labeled intermediates and crystal structures of SAM-bound CmnDph2. EPR and ENDOR spectra of isotope-labeled intermediates."— Presentation transcript:

1 Fig. 3 EPR and ENDOR spectra of isotope-labeled intermediates and crystal structures of SAM-bound CmnDph2. EPR and ENDOR spectra of isotope-labeled intermediates and crystal structures of SAM-bound CmnDph2. (A) 35 GHz CW 13C ENDOR spectra for intermediate I with (methionine-13C5)–SAM. (B) Isotope EPR study of the organic radical intermediate II on EF2 quenched at 2 min (T = 70 K). Intensity adjusted for comparison. (C) Cluster and bound SAM in the structure of CmnDph2 (left), in comparison with cluster and bound SAM in the structure of PFL-AE (right, PDB 3CB8) (13). Distances are given in angstroms. The black and brown asterisks label Cγ,Met of SAM and the differentiated iron of the [4Fe-4S] cluster, respectively. (D) Overlay of SAM and cluster in CmnDph2 and PFL-AE structures. (E) CmnDph2 active site showing the binding of SAM. Hydrophobic interactions with purine ring of SAM are not shown for clarity. Min Dong et al. Science 2018;359: Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works

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