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Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans

Lesley Tilleman ; Stefania Abbruzzetti ; Chiara Ciaccio ; Giampiero De Sanctis ; Marco Nardini ; Alessandra Pesce ; Filip Desmet ; Luc Moens ; Sabine Van Doorslaer ; Stefano Bruno ; Martino Bolognesi ; Paolo Ascenzi ; Massimo Coletta ; Cristiano Viappiani ; Sylvia Dewilde

PloS one, 01 January 2015, Vol.10(6), p.e0125959 [Tạp chí có phản biện]

E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0125959

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  • Nhan đề:
    Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans
  • Tác giả: Lesley Tilleman ; Stefania Abbruzzetti ; Chiara Ciaccio ; Giampiero De Sanctis ; Marco Nardini ; Alessandra Pesce ; Filip Desmet ; Luc Moens ; Sabine Van Doorslaer ; Stefano Bruno ; Martino Bolognesi ; Paolo Ascenzi ; Massimo Coletta ; Cristiano Viappiani ; Sylvia Dewilde
  • Chủ đề: Sciences (General)
  • Là 1 phần của: PloS one, 01 January 2015, Vol.10(6), p.e0125959
  • Mô tả: Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb*, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb*. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb*. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb* and by the CO dissociation rate constants....
  • Ngôn ngữ: English
  • Số nhận dạng: E-ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0125959

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