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Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin.(Research Article)

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

PLoS ONE, March 27, 2012, Vol.7(3), p.e33614 [Tạp chí có phản biện]

ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0033614

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  • Nhan đề:
    Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin.(Research Article)
  • Tác giả: Abbruzzetti, Stefania ; Tilleman, Lesley ; Bruno, Stefano ; Viappiani, Cristiano ; Desmet, Filip ; Van Doorslaer, Sabine ; Coletta, Massimo ; Ciaccio, Chiara ; Ascenzi, Paolo ; Nardini, Marco ; Bolognesi, Martino ; Moens, Luc ; Dewilde, Sylvia
  • Chủ đề: Hemoglobins -- Analysis ; Heme -- Analysis
  • Là 1 phần của: PLoS ONE, March 27, 2012, Vol.7(3), p.e33614
  • Mô tả: Protoglobin from Methanosarcina acetivorans (MaPgb) is a dimeric globin with peculiar structural properties such as a completely buried haem and two orthogonal tunnels connecting the distal cavity to the solvent. CO binding to and dissociation from MaPgb occur through a biphasic kinetics. We show that the heterogenous kinetics arises from binding to (and dissociation from) two tertiary conformations in ligation-dependent equilibrium. Ligation favours the species with high binding rate (and low dissociation rate). The equilibrium is shifted towards the species with low binding (and high dissociation) rates for the unliganded molecules. A quantitative model is proposed to describe the observed carbonylation kinetics.
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 1932-6203 ; DOI: 10.1371/journal.pone.0033614

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