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- Title
Structural analysis of zinc-substituted cytochrome c.
- Authors
Chengmin Qian; Yong Yao; Yufeng Tong; Jinfeng Wang; Wenxia Tang
- Abstract
abstract zinc-substituted cytochrome c has been widely used in studies of protein-protein interactions and photo-induced electron transfer reactions between proteins. however, the coordination geometry of zinc in zinc-substituted cyt c has not yet been determined; two different opinions about the coordination have been reached. here the solution structures of zinc-substituted cytochrome c that might be five-coordinated and six-coordinated have been refined separately by using 1h nmr spectroscopy, and the zinc coordination geometry was determined just by noe distance constraints. structural analysis of the energy-minimized average solution structures of both the pentacoordinated and hexacoordinated geometries indicate that that zinc in zinc-substituted cyt c should be bound to both his18 and met80, which means that the zinc is six-coordinated. rmsd values of the family of 25 six-coordinated structures from the average structure are 0.66±0.13 å and 1.09±0.16 å for the backbone and all heavy atoms, respectively. a statistical analysis of the structure indicates its satisfactory quality. comparison of the solution structure of the six-coordinated energy-minimized average structure of zinc-substituted cytochrome c with the solution structure of reduced cytochrome c reveals that for the overall folding the secondary structure elements are very close. the availability of the structure provides for a better understanding of the protein-protein complex and for electron transfer processes between zn cyt c and other metalloproteins.
- Subjects
CYTOCHROME c; ZINC; SUBSTITUTION reactions
- Publication
Journal of Biological Inorganic Chemistry (JBIC), 2003, Vol 8, Issue 4, p394
- ISSN
0949-8257
- Publication type
Article
- DOI
10.1007/s00775-002-0428-1