ログイン
言語:

WEKO3

  • トップ
  • ランキング
To
lat lon distance
To

Field does not validate



インデックスリンク

インデックスツリー

メールアドレスを入力してください。

WEKO

One fine body…

WEKO

One fine body…

アイテム

  1. B. 理工学域; 数物科学類・物質化学類・機械工学類・フロンティア工学類・電子情報通信学類・地球社会基盤学類・生命理工学類
  2. b 10. 学術雑誌掲載論文
  3. 1.査読済論文(理)

Intermediate and mechanism of hydroxylation of o-iodophenol by salicylate hydroxylase

http://hdl.handle.net/2297/14573
http://hdl.handle.net/2297/14573
6f69e03f-2994-4340-a689-1534bb3fc057
名前 / ファイル ライセンス アクション
SC-PR-ITAGAKI-E-791.pdf SC-PR-ITAGAKI-E-791.pdf (1.1 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-10-03
タイトル
タイトル Intermediate and mechanism of hydroxylation of o-iodophenol by salicylate hydroxylase
言語 en
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
著者 Suzuki, Kenzi

× Suzuki, Kenzi

WEKO 15573

Suzuki, Kenzi

Search repository
Gomi, Tomoharu

× Gomi, Tomoharu

WEKO 15574

Gomi, Tomoharu

Search repository
Itagaki, Eiji

× Itagaki, Eiji

WEKO 15575

Itagaki, Eiji

Search repository
著者別名 板垣, 英治

× 板垣, 英治

WEKO 15084

板垣, 英治

Search repository
提供者所属
内容記述タイプ Other
内容記述 金沢大学自然科学研究科
提供者所属
内容記述タイプ Other
内容記述 金沢大学理工研究域自然システム学系
書誌情報 Journal of Biochemistry

巻 109, 号 5, p. 791-797, 発行日 1991-01-01
ISSN
収録物識別子タイプ ISSN
収録物識別子 0021-924X
NCID
収録物識別子タイプ NCID
収録物識別子 AA00694073
出版者
出版者 日本生化学会 = Japanese Biochemical Society
抄録
内容記述タイプ Abstract
内容記述 Salicylate hydroxylase [EC 1.14.13.1] from Pseudomonas putida catalyzes the hydroxylation of salicylate, and also o-aminophenol, o-nitrophenol, and o-halogenophenols, to catechol. The reactions with these o-substituted phenols comprise oxygenative deamination, denitration, and dehalogenation, respectively. The reaction try, as to NADH oxidized, oxygen consumed, and catechol formed, is 2 : 1 : 1, respectively. The mechanisms for the deiodination and oxygenation of o-iodophenol were investigated in detail by the use of I+-trapping reagents such as DL-methionine, 2-chlorodimedone, and L-tyrosine. The addition of the traps did not change the molar ratio of catechol formed to NADH oxidized, nor iodinated traps produced were in the incubation mixture. The results suggest that I+ was not produced on the deiodination in the hydroxylation of o-iodophenol. On the other hand, L-ascorbate, L-epinephrine, and phenylhydrazine increased the molar ratio. o-Phenylenediamine decreased it, being converted to phenazine. This suggests that o-benzoquinone is formed in the oxidation of o-iodophenol as a nascent product. The quinone was detected spectrophotometrically by means of the stopped-flow method. Kinetic analysis of the reactions revealed that o-benzoquinone is reduced nonenzymatically to catechol by a second molecule of NADH. A mechanism of elimination for the ortho-substituted groups of substrate phenols by the enzyme is proposed and discussed.
権利
権利情報 Copyright © 1991 Japanese Biochemical Society
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連URI
関連タイプ isIdenticalTo
識別子タイプ URI
関連識別子 http://jb.oxfordjournals.org/cgi/content/abstract/109/5/791
関連URI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 https://doi.org/10.1093/oxfordjournals.jbchem.a123458
戻る
0
views
See details
Views

Versions

Ver.1 2023-07-27 09:32:43.617451
Show All versions

Share

Mendeley Twitter Facebook Print Addthis

Cite as

エクスポート

OAI-PMH
  • OAI-PMH JPCOAR 2.0
  • OAI-PMH JPCOAR 1.0
  • OAI-PMH DublinCore
  • OAI-PMH DDI
Other Formats
  • JSON
  • BIBTEX

Confirm


Powered by WEKO3


Powered by WEKO3