Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin (Articolo in rivista)

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  • Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1371/journal.pone.0033614 (literal)
Alternative label
  • Abbruzzetti, S; Tilleman, L; Bruno, S; Viappiani, C; Desmet, F; Van Doorslaer, S; Coletta, M; Ciaccio, C; Ascenzi, P; Nardini, M; Bolognesi, M; Moens, L; Dewilde, S (2012)
    Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin
    in PloS one
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Abbruzzetti, S; Tilleman, L; Bruno, S; Viappiani, C; Desmet, F; Van Doorslaer, S; Coletta, M; Ciaccio, C; Ascenzi, P; Nardini, M; Bolognesi, M; Moens, L; Dewilde, S (literal)
Pagina inizio
  • e33614 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 7 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Parma, Dipartimento Fis, I-43100 Parma, Italy Ist Nanoscienze CNR, NEST, Pisa, Italy Univ Antwerp, Dept Biomed Sci, B-2020 Antwerp, Belgium Univ Parma, Dipartimento Biochim & Biol Mol, I-43100 Parma, Italy Univ Antwerp, Dept Phys, B-2020 Antwerp, Belgium Univ Roma Tor Vergata, Dipartimento Sci Clin & Med Traslazionale, Rome, Italy Consorzio Interuniversitario Ric Chim Met Sistemi, Bari, Italy Univ Roma, Dipartimento Biol, Rome, Italy Univ Milan, Dipartimento Sci Biomol & Biotecnol, I-20122 Milan, Italy Univ Milan, CIMAINA, I-20122 Milan, Italy (literal)
Titolo
  • Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin (literal)
Abstract
  • 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. (literal)
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