@article{oai:tsukuba.repo.nii.ac.jp:00027214,
 author = {太, 虎林 and 山本, 泰彦 and Tai, Hulin and Udagawa, Tsuyoshi and Mikami, Shin-ichi and Sugimoto, Akihiro and Yamamoto, Yasuhiko},
 journal = {Journal of inorganic biochemistry},
 month = {Mar},
 note = {Pseudomonasaeruginosacytochromec551 (PA) possesses a long polypeptideloop near its heme, and a unique hydrogen bond network among Ser52, axial Met61, and the heme 13-propionate side chain, i.e., Ser52 amide NH is hydrogen bonded to axial Met61 carbonyl CO, Met61 amide NH to Ser52 carbonyl CO, and Ser52 side chain OH to the heme 13-propionate side chain, contributes to stabilization of the structure of the loop [Y. Matsuura, T. Takano, R.E. Dickerson, J. Mol. Biol. 156 (1982) 389–409]. In this study, the structure and redoxfunction of S52N and S52G mutants were characterized in order to elucidate the role of Ser52 in functional regulation of the protein. We found that the redoxfunction of PA was hardly affected by an S52N mutation, but was slightly by an S52G one. The functional similarity between the wild-type protein and the S52N mutant demonstrated that Asn52 in the mutant plays a similar pivotal role in the formation of the unique hydrogen bond network that stabilizes the structure of the loop as Ser52 in the wild-type protein does. On the other hand, the functional alteration induced by the S52G mutation can be attributed to astructural change of the loop due to the lack of the hydrogen bond between the Gly52 and heme 13-propionate side chain in the mutant. Thus, this study demonstrated that the function of the protein can be tuned through the structuralproperties of the polypeptideloop near its heme.},
 pages = {182--187},
 title = {Finetuning of the redoxfunction of Pseudomonasaeruginosacytochromec551 through structuralproperties of apolypeptideloopbearing an axialMetresidue},
 volume = {108},
 year = {2012}
}