tailieunhanh - Báo cáo khoa học: Cytoglobin conformations and disulfide bond formation

The oligomeric state and kinetics of ligand binding were measured for wild-type cytoglobin. Cytoglobin has the classical globin fold, with an extension at each extremity of about 20 residues. The extended length of cytoglobin leads to an ambiguous interpretation of its oligomeric state. | ễFEBS Journal Cytoglobin conformations and disulfide bond formation Christophe Lechauve1 Cedric Chauvierre1 Sylvia Dewilde2 Luc Moens2 Brian N. Green3 Michael C. Marden1 Chantal Celier1 and Laurent Kiger1 1 Inserm U779 Universities Paris VI et XI Le Kremlin-Bicetre France 2 Department of BiomedicalSciences University of Antwerp Belgium 3 Waters MS Technologies Centre Micromass UK Ltd. Altrincham Cheshire UK Keywords disulfides globins kinetics ligand binding light scattering Correspondence L. Kiger INSERM - U779 78 rue du GeneralLeclerc Hopitalde Bicetre Bat. Broca Niveau 3 94275 Le Kremlin Bicetre France Fax 33 1 49 59 56 61 Tel 33 1 49 59 56 64 E-mail Received 18 February 2010 revised 8 April 2010 accepted 13 April 2010 doi The oligomeric state and kinetics of ligand binding were measured for wild-type cytoglobin. Cytoglobin has the classical globin fold with an extension at each extremity of about 20 residues. The extended length of cytoglobin leads to an ambiguous interpretation of its oligomeric state. Although the hydrodynamic diameter corresponds to that of a dimer it displays a mass of a single subunit indicating a monomeric form. Thus rather than displaying a compact globular form cytoglobin behaves hydrodynamically like a tightly packed globin with a greater flexibility of the N- and C-terminal regions. Cytoglobin displays biphasic kinetics after the photolysis of CO as a result of competition with an internal protein ligand the E7 distal histidine. An internal disulfide bond may form which modifies the rate of dissociation of the distal histidine and apparently leads to different cytoglobin conformations which may affect the observed oxygen affinity by an order of magnitude. Introduction The vertebrate heme globin family has been extended to include two new members neuroglobin Ngb and cytoglobin Cygb which differ in structure tissue distribution and function 1-3 . Cygb is expressed at varying .

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