@article{oai:shinshu.repo.nii.ac.jp:00022572,
 author = {MIHARA, MASASHI and KOMACHIYA, MIHO and MIZOUE, SHINYA and OSAWA, MASAKI and UEMATSU, SETSUKO and KIKUCHI, YUICHIRO and OKUBO, YUICHIRO and HIRAI, KANAME and KUROIWA, AKIHIRO and YAMADA, KAZUHIRO and YAMAKURA, FUMIYUKI and HIRAOKA, B.YUKIHIRO and 三原, 正志 and 小町谷, 美帆 and 溝上, 真也 and 大澤, 雅樹 and 上松, 節子 and 菊池, 有一郎 and 大久保, 裕一郎 and 平井, 要 and 黒岩, 昭弘 and 山田, 一尋 and 山倉, 文幸 and 平岡, 行博},
 issue = {1},
 journal = {松本歯学, Journal of the Matsumoto Dental University Society},
 month = {Jun},
 note = {The role of superoxide dismutase (SOD) as a radical scavenger in Porphyromonas gingivalis is well documented. P. gingivalis SOD (Pg SOD), which is characterized by a metal–tolerant activity, can use either iron or manganese as a cofactor. Leu ₇2 and Leu ₇6, located near the active–site metal, are characteristic amino acid sequences of Pg SOD proteins, although they are substituted to Trp in the ₇2 position and Phe in the ₇6 position in most iron–containing SOD (Fe–SOD) proteins. In the present study, we constructed a mutant of the enzyme with changes from Leu ₇2 to Trp and Leu ₇6 to Phe. This mutant SOD was examined with respect to its metal–dependent activity and structural characterization. We herein conclude the integrity of Leu ₇2 and Leu ₇6 is a necessary requisite for the metal–tolerant activity of Pg SOD., application/pdf},
 pages = {26--34},
 title = {Contribution of the amino acid residues located near the active site metal to the metal–specific activity of Porphyromonas gingivalis SOD induced by a double mutation of Leu 72 Trp and Leu 76 Phe},
 volume = {40},
 year = {2014}
}