Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c

FEBS Letters

Davies, Anne M.¹  Thurgood, Andrew G.P.²  Grant Mauk, A.³  Moore, G.R.²  Pielak, Gary J.⁴  Cutler, Robert L.³  Greenwood, Colin¹  Williamson, David J.²  Smith, Michael³ 

[1] Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich, NR4 7TJ, UK;Centre for Metalloprotein Spectroscopy and Biology, School of Chemical Sciences, University of East Anglia, Norwich, NR4 7TJ, UK;Department of Biochemistry, University of British Columbia, Vancouver, British Columbia, VT6 1W5, Canada;Inorganic Chemistry Laboratory, University of Oxford, Oxford OX1 3QR, UK

关键词: Yeast cytochrome c;    Mutagenesis;    1H-NMR;    COSY;    NOE;   

DOI  :  10.1016/0014-5793(91)80678-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The only significant area of conformational change detected was at residues 39 and 58, close to the site of modification. Therefore the redox potential change accompanying the modification [1988, Biochemistry 28, 3198–3197] appears to be a direct consequence of the altered side-chain of residue 38 and not a result of secondary conformational changes induced by the modification.

【 授权许可】

Unknown