A quantum mechanical study of the transfer of biological sulfate

Lee Bartolotti, Yoshimitsu Kakuta, Lars Pedersen, Masahiko Negishi, Lee Pedersen

研究成果: Contribution to journalArticle査読

7 被引用数 (Scopus)

抄録

The biological process of enzymatic sulfuryl group transfer has been studied by ab initio (density-functional and Hartree-Fock) and semiempirical quantum mechanical methods. The active site of estrogen sulfotransferase in ternary complex with a sulfate donor (PAPS) and sulfate acceptor (estradiol) is modeled. The mechanism proposed in a recent X-ray crystal structure paper (Kakuta et al., Nat. Struct. Biol. 4 (1997) 904) serves as the basis for the calculations. We find that the mechanism proposed in the crystallographic paper is reasonable. The sulfonation takes place in several key steps: neutralization of the charge on PAPS, lengthening of the bridging S-O bond with no cost in energy, activation of the attacking oxygen and proton transfer from estradiol to histidine and then to the sulfuryl group.

本文言語英語
ページ(範囲)105-111
ページ数7
ジャーナルJournal of Molecular Structure: THEOCHEM
461-462
DOI
出版ステータス出版済み - 4 2 1999
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 凝縮系物理学
  • 物理化学および理論化学

フィンガープリント

「A quantum mechanical study of the transfer of biological sulfate」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

引用スタイル