Investigation of oxidation state‐dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome C 553 by two‐dimensional 1H‐NMR spectra

FEBS Letters

Guerlesquin, Françoise¹  Blanchard, Laurence¹  Blackledge, Martin J.²  Marion, Dominique² 

[1] Laboratoire de Bioenérgétique et Ingénierie des Protéines, CNRS, 13402 Marseille Cedex 20, France;Laboratoire de Résonance Magnétique Nucléaire, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA, 38027 Crenoble Cedex 1, France

关键词: Ferricytochrome c 553;    Desulfovibrio;    Two-dimensional NMR;    Paramagnetic shift;    Low oxidoreduction potential;    1D/2D;    one/two-dimensional;    TOCSY;    total correlation spectroscopy;    COSY;    correlation spectroscopy;    DQF-COSY;    double quantum filtered correlation spectroscopy;    NOESY;    nuclear Overhauser effect spectroscopy;   

DOI  :  10.1016/0014-5793(96)00580-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR) was used to assign the proton resonances of ferricytochrome C ₅₅₃ from Desulfovibrio vulgaris Hildenborough. The spin systems of 76 out of 79 amino acids were identified by J-correlation spectroscopy (COSY and HOHAHA) in H₂O and D₂O and correlated by nuclear Overhauser effect spectroscopy (NOESY). The proton chemical shifts are compared in both oxidized and reduced states of the protein at 23°C and pH 5.9. Chemical shift variations between reduced and oxidized states are due to the paramagnetic contribution. Medium and longrange nOe demonstrate the lack of major changes between the two redox states. NMR data provide evidence that in this low oxidoreduction potential cytochrome, the oxidized state is more rigid than the reduced state.

【 授权许可】

Unknown