The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 (Articolo in rivista)

Type
Label
  • The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 (Articolo in rivista) (literal)
Anno
  • 2011-01-01T00:00:00+01:00 (literal)
Alternative label
  • Howes BD1, Giordano D2, Boechi L3, Russo R3, Mucciacciaro S1, Ciaccio C4,5, Sinibaldi F4, Fittipaldi M1,6, Martí MA3, Estrin DA3, di Prisco G2, Coletta M4,5, Verde C2, Smulevich G1,5 (2011)
    The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125
    in JBIC. Journal of biological inorganic chemistry (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Howes BD1, Giordano D2, Boechi L3, Russo R3, Mucciacciaro S1, Ciaccio C4,5, Sinibaldi F4, Fittipaldi M1,6, Martí MA3, Estrin DA3, di Prisco G2, Coletta M4,5, Verde C2, Smulevich G1,5 (literal)
Pagina inizio
  • 299 (literal)
Pagina fine
  • 311 (literal)
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  • 16 (literal)
Rivista
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  • PMID: 21076847 http://www.springerlink.com/content/j71778813264xx12/ (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • 1 Dipartimento di Chimica, Universita` di Firenze, 50019 Sesto Fiorentino (FI), Italy 2 Institute of Protein Biochemistry, CNR, 80131 Naples, Italy 3Departemento de Qu?´mica Inorga´nica,Anal?´tica y Qu?´mica F?´sica/INQUIMAE-CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, C1428EHA Buenos Aires, Argentina 4 Dipartimento di Medicina Sperimentale e Scienze Biochimiche, Universita` di Roma Tor Vergata, 00133 Rome, Italy 5 Consorzio Interuniversitario di Ricerca in Chimica dei Metalli nei Sistemi Biologici, 70126 Bari, Italy 6INSTM (Consorzio Interuniversitario per la Scienza e Tecnologia dei Materiali), 50019 Sesto Fiorentino (FI), Italy (literal)
Titolo
  • The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125 (literal)
Abstract
  • The genome of the cold-adapted bacterium Pseudoalteromonas haloplanktis TAC125 contains multiple genes encoding three distinct monomeric hemoglobins exhibiting a 2/2 ±-helical fold. In the present work, one of these hemoglobins is studied by resonance Raman, electronic absorption and electronic paramagnetic resonance spectroscopies, kinetic measurements, and different bioinformatic approaches. It is the first cold-adapted bacterial hemoglobin to be characterized. The results indicate that this protein belongs to the 2/2 hemoglobin family, Group II, characterized by the presence of a tryptophanyl residue on the bottom of the heme distal pocket in position G8 and two tyrosyl residues (TyrCD1 and TyrB10). However, unlike other bacterial hemoglobins, the ferric state, in addition to the aquo hexacoordinated high-spin form, shows multiple hexacoordinated low-spin forms, where either TyrCD1 or TyrB10 can likely coordinate the iron. This is the first example in which both TyrCD1 and TyrB10 are proposed to be the residues that are alternatively involved in heme hexacoordination by endogenous ligands. (literal)
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