The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket (Articolo in rivista)

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  • The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • Ilari A. 1, Bonamore A. 2, Farina A. 2, Johnson K. A. 2, Boffi A.2 (2002)
    The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket
    (literal)
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  • Ilari A. 1, Bonamore A. 2, Farina A. 2, Johnson K. A. 2, Boffi A.2 (literal)
Pagina inizio
  • 23725 (literal)
Pagina fine
  • 23732 (literal)
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  • The work has biotechnological implications due to the possible involvement of HMP in membrane phospholipids redox modifications. The manuscript is published in a highly valued international scientific journal (impact factor of 7,258). The paper has been cited 9 times in international scientific journals. (literal)
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  • 277 (literal)
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  • A. Boffi incaricato di ricerca (literal)
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  • The X-ray structure of ferric Escherichia coli flavohemoglobin (HMP) reveals an unexpected geometry of the distal heme pocket . The structural features are strongly suggestive of a peroxidase-like site where the proximal histidine is endowed with a significant imidazolate character. Based on the structural and functional data, a model is presented that explains the lipid binding properties of HMP and other members of the flavohemoglobin family and is strongly suggestive of similar function(s) in the whole bacterial haemoglobin superfamily. (literal)
Note
  • ISI Web of Science (WOS) (literal)
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  • 1 CNR (C.S. sulla Biologia Molecolare) 2 Uni Sapienza (Dipartimento di Scienze Biochimiche \"A. Rossi Fanelli\") (literal)
Titolo
  • The X-ray structure of ferric Escherichia coli flavohemoglobin reveals an unexpected geometry of the distal heme pocket (literal)
Abstract
  • The x-ray structure of ferric unliganded lipid-free Escherichia coli flavohemoglobin has been solvedto a resolution of 2.2 A and refined to an R-factor of 19%. The overall fold is similar to that of ferrous lipid-bound Alcaligenes eutrophus flavohemoglobin with the notable exception of the E helix positioning within the globin domain and a rotation of the NAD binding module with respect to the FAD-binding domain accompanied by a substantial rearrangement of the C-terminal region. An inspection of the heme environment in E. coli flavohemoglobin reveals an unexpected architecture of the distal pocket. In fact, the distal site is occupied by the isopropyl side chain Leu-E11 that shields the heme iron from the residues in the topological positions predicted to interact with heme iron-bound ligands, namely Tyr-B10 and Gln-E7, and stabilizes a pentacoordinate ferric iron species. Ligand binding properties are consistent with the presence of a pentacoordinate species in solution as indicated by a very fast second order combination rates with imidazole and azide. Surprisingly, imidazole, cyanide, and azide binding profiles at equilibrium are not accounted for by a single site titration curve but are biphasic and strongly suggest the presence of two distinct conformers within the liganded species. (literal)
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