Premium
Investigation of oxidation state‐dependent conformational changes in Desulfovibrio vulgaris Hildenborough cytochrome C 553 by two‐dimensional 1 H‐NMR spectra
Author(s) -
Blanchard Laurence,
Blackledge Martin J.,
Marion Dominique,
Guerlesquin Françoise
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00580-7
Subject(s) - desulfovibrio vulgaris , chemistry , nuclear overhauser effect , nuclear magnetic resonance spectroscopy , two dimensional nuclear magnetic resonance spectroscopy , spectroscopy , chemical shift , proton , crystallography , nmr spectra database , nuclear magnetic resonance , analytical chemistry (journal) , spectral line , stereochemistry , organic chemistry , physics , genetics , quantum mechanics , astronomy , bacteria , biology
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 H 2 O and D 2 O 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.