Analysis of Rate-determining Factors in the Oxidative Reaction of Monolignols by Peroxidase-H<SUB>2</SUB>O<SUB>2</SUB> System
スポンサーリンク
概要
- 論文の詳細を見る
The rate constants were experimentally obtained for the oxidative reaction of three monolignols (<I>p</I>-coumaryl, coniferyl and sinapyl alcohol) and four similar forms of 3-mono- or 3, 5-disubstituted <I>p</I>-coumaryl alcohols (3-ethoxy-, 3-propoxy-, 3-methyl- and 3, 5-dimethyl-<I>p</I>-coumaryl alcohol) by using horseradish peroxidase (HRP) -H<SUB>2</SUB>O<SUB>2</SUB> as the oxidant. To investigate the factor determining reaction rate of each substrate, the molecular volume and the highest occupied molecular orbital (HOMO) energy were applied. The molecular volume was obtained by using optimum conformation data with MOPAC2000. And the HOMO energy was calculated with MOPAC2000 under four conditions, i.e., when the phenolic hydroxyl form of each compound is either neutral or anion, and when each substrate is at polar or nonpolar milieu.<BR>We infer that the reason why 3, 5-disubstituted <I>p</I>-coumaryl alcohol deviates from the profiles of others was due to local steric hindrance and distortion effect of the substituted groups. In assuming anion/water, the reaction rates of substrates correlated with HOMO energies excluding 3, 5-disubstituted <I>p</I>-coumaryl alcohols. In alternate form and milieu, no suitable relationship between HOMO energies and reaction rates was obtained. From these results, we suggest that the rate-determining step in the oxidative reaction for 3-substituted <I>p</I>-coumaryl alcohol is where one electron is withdrawn by oxidized HRP under anion/water condition.
- 日本コンピュータ化学会の論文
日本コンピュータ化学会 | 論文
- 計算機シミュレーションを用いたRNA結合タンパク質PumilioのRNA結合様式の研究
- エストロゲン受容体のアミノ酸変異によるエストラジオール結合エネルギーの変化
- 分割法による大規模共役系のケクレ構造の総数とPauling Bond Orderの計算
- SrTiO_3とCaTiO_3のTi-K XANESスペクトルにおける低エネルギーピークの起源
- 分子骨格操作に伴う分子軌道変化の等値面リアルタイム描画システム