Ligand and proton linked conformational changes of ferrous 2/2 hemoglobin of Pseudoalteromonas haloplantktis TAC 125 (Articolo in rivista)

Type
Label
  • Ligand and proton linked conformational changes of ferrous 2/2 hemoglobin of Pseudoalteromonas haloplantktis TAC 125 (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Alternative label
  • Daniela Giordano1, Roberta Russo1, Chiara Ciaccio2,3, Barry D. Howes4, Guido di Prisco1, Michael C. Marden5, Gaston Hui Bon Hoa5, Giulietta Smulevich4, Massimo Coletta2,3 and Cinzia Verde1 (2011)
    Ligand and proton linked conformational changes of ferrous 2/2 hemoglobin of Pseudoalteromonas haloplantktis TAC 125
    in IUBMB life (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Daniela Giordano1, Roberta Russo1, Chiara Ciaccio2,3, Barry D. Howes4, Guido di Prisco1, Michael C. Marden5, Gaston Hui Bon Hoa5, Giulietta Smulevich4, Massimo Coletta2,3 and Cinzia Verde1 (literal)
Pagina inizio
  • 566 (literal)
Pagina fine
  • 573 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 63 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#note
  • PMID: 21698762 http://onlinelibrary.wiley.com/doi/10.1002/iub.492/abstract (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1Institute of Protein Biochemistry, CNR, Naples, Italy 2Department of Experimental Medicine and Biochemical Sciences, Universita` di Roma Tor Vergata, Rome, Italy 3Interuniversity Consortium for the Research on the Chemistry of Metals in Biological Systems, Bari, Italy 4Dipartimento di Chimica ''Ugo Schiff'', Universita` di Firenze, Sesto Fiorentino (FI), Italy 5INSERM, U779, 78 rue du General Leclerc, Le Kremlin Bicetre, France (literal)
Titolo
  • Ligand and proton linked conformational changes of ferrous 2/2 hemoglobin of Pseudoalteromonas haloplantktis TAC 125 (literal)
Abstract
  • The spectroscopic and ligand-binding properties of a 2/2 globin from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125 have been studied in the ferrous state. It displays two major conformations characterized by CO-association rates that differ by a factor of 20, with relative fractions that depend on pH. A dynamic equilibrium is found between the two conformations, as indicated by an enhanced slower phase when lower CO levels were used to allow a longer time to facilitate the transition. The deoxy form, in the absence of external ligands, is a mixture of a predominant six-coordinate low spin form and a five-coordinate high-spin state; the proportion of low spin increasing at alkaline pH. In addition, at temperatures above the physiological temperature of 1 °C, an enhanced tendency of the protein to oxidize is observed. (literal)
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