The influence of Glu44 and Glu56 of cytochrome b5 on the protein structure and interaction with cytochrome c |
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Authors: | Sun Yu-Long; Xie Yi; Wang Yun-Hua; Xiao Gu-Tian; Huang Zhong-Xian |
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Affiliation: | Department of Chemistry, Fudan University Shanghai, PRC 200433
1Institute of Genetics, Fudan University Shanghai, PRC 200433 |
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Abstract: | The gene encoding trypsin-solubilized bovine liver microsomalcytochrome b5 (82 residues in length) has been mutated, in whichthe codons of Glu44 and Glu56 were changed to those of Ala.The mutated genes were expressed in Escherichia coli successfullyand three mutant proteins (E44A, E56A and E44/56A) were obtained.The UV-visible, CD and 1H NMR spectra of proteins have beenstudied. The results show that the mutagenesis at surface residuesdoes not alter the secondary and tertiary structures of cytochromeb5 significantly. The interactions between recombinant cytochromeb5 and its mutants with cytochrome c were studied by using opticaldifference spectra. The results demonstrated that both Glu44and Glu56 of cytochrome b5 participate in the formation of acomplex between cytochrome b5 and cytochrome c. |
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Keywords: | cytochrome b5 c complex/ mutagenesis/ protein structure |
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