Effects of Mutations of Lys41 and Asp102 of Bacteriorhodopsin

• ZHAO Yingchun

  Key Laboratory of Molecular Engineering of Polymers of the Ministry of Education, Department of Macromolecular Science, Laboratory of Advanced Materials, Fudan University Department of Biochemistry, School of Life Sciences, Fudan University

• WANG Yazhuo

  Key Laboratory of Molecular Engineering of Polymers of the Ministry of Education, Department of Macromolecular Science, Laboratory of Advanced Materials, Fudan University

• MA Dewang

  Key Laboratory of Molecular Engineering of Polymers of the Ministry of Education, Department of Macromolecular Science, Laboratory of Advanced Materials, Fudan University

• WU Jia

  Key Laboratory of Molecular Engineering of Polymers of the Ministry of Education, Department of Macromolecular Science, Laboratory of Advanced Materials, Fudan University

• HUANG Weida

  Department of Biochemistry, School of Life Sciences, Fudan University

• DING Jiandong

  Key Laboratory of Molecular Engineering of Polymers of the Ministry of Education, Department of Macromolecular Science, Laboratory of Advanced Materials, Fudan University

抄録

Bacteriorhodopsin (BR) is a retinal protein that functions as a light-driven proton pump. In this study, six novel mutants including K41E and D102K, were obtained to verify or rule out the possibility that residues Lys41 and Asp102 are determinants of the time order of proton release and uptake, because we found that the order was reversed in another retinal protein archaerhodopsin 4 (AR4), which had different 41th and 102th residues. Our results rule out that possibility and confirm that the pK_a of the proton release complex (PRC) determines the time order. Nevertheless, mutations, especially D102K, were found to affect the kinetics of proton uptake substantially and the pK_a of Asp96. Compared to the wild-type BR (BR-WT), the decay of the M intermediate and proton uptake in the photocycle was slowed about 3-fold in D102K. Hence those residues might be involved in proton uptake and delivery to the internal proton donor.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 75 (7), 1364-1370, 2011

  公益社団法人 日本農芸化学会

キーワード

• bacteriorhodopsin
• point mutant
• proton pump
• M decay

詳細情報

• CRID: 1390282681453632000
• NII論文ID: 10029329432
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.110180
• ISSN: 13476947
• ISSN: 09168451
• NDL書誌ID: 11175123
• PubMed: 21737924
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I11175123
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.110180
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可