2-((6E,10E,14E)-3,7,11,15,19-Pentamethyl-icosa-6,10,14,18-tetraenyloxy)-phenazine

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: 2-((6E,10E,14E)-3,7,11,15,19-Pentamethyl-icosa-6,10,14,18-tetraenyloxy)-phenazine
• 英文别名: Methanophenazine；2-[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraenoxy]phenazine
• 化学式: C₃₇H₅₀N₂O
• 分子量: 538.817
• InChiKey: VRHMBACMYZITGD-QAAQOENVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  11.8
• 重原子数：
  40
• 可旋转键数：
  16
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.46
• 拓扑面积：
  35
• 氢给体数：
  0
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  氢气 、 2-((6E,10E,14E)-3,7,11,15,19-Pentamethyl-icosa-6,10,14,18-tetraenyloxy)-phenazine 生成 Dihydromethanophenazine
  参考文献：
  名称：

  Isolation and Characterization of Methanophenazine and Function of Phenazines in Membrane-Bound Electron Transport ofMethanosarcina mazeiGö1

  摘要：

  摘要：通过异辛烷萃取，从冻干的Methanosarcina mazeiGö1 膜中分离出一种疏水性氧化还原活性成分，其分子质量为 538 Da。经高效液相色谱柱纯化后，通过质谱和核磁共振研究分析了其化学结构。这种成分被称为甲吩嗪，是一种 2-羟基吩嗪衍生物，通过醚桥与多异戊烯侧链相连。由于甲基吩嗪几乎不溶于水性缓冲液，因此我们测试了水溶性吩嗪衍生物与参与电子传递和能量守恒的膜结合酶相互作用的能力。从 M. mazeiGö1 中纯化的 F420H2 脱氢酶在加入 2-羟基吩嗪和 2-溴吩嗪作为电子受体时显示出最高的活性。酚嗪-1-羧酸和酚嗪的活性较低。2- 羟基哒嗪和吩嗪的 Km 值分别为 35 μM 和 250 μM。2- 羟基哒嗪也在一种 F420 非反应性氢化酶的催化下被分子氢还原，这种氢化酶存在于洗膜制备物中。此外，膜结合的杂二硫还原酶能够利用还原的 2-羟基哒嗪作为电子供体，还原 CoB-S-S-CoM。考虑到所有这些结果，我们有理由推测甲氧苄肼在马泽Gö1的膜结合电子传递过程中发挥了重要作用。

  DOI：

  10.1128/jb.180.8.2027-2032.1998
• 作为产物：
  描述：

  (3E,7E,11E,15E)-4,8,12,16,20-Pentamethyl-henicosa-3,7,11,15,19-pentaen-1-ol 在 氢氧化钾 作用下， 以 四氢呋喃 、 二氯甲烷 为溶剂， 生成 2-((6E,10E,14E)-3,7,11,15,19-Pentamethyl-icosa-6,10,14,18-tetraenyloxy)-phenazine
  参考文献：
  名称：

  甲氧吩嗪：产甲烷古细菌中新辅因子的结构，总合成和功能这项工作得到了德国科学基金会的支持（Sonderforschungsbereich 416；授予488 / 6-1和De 488 / 4-2）和Foinds der Chemischen Industrie。我们感谢博士。J. Paust和H. Jaedicke（路德维希港的BASF AG）和RKMüller博士（巴塞尔的Hoffmann-La Roche Ltd.）慷慨地提供化学品。

  摘要：

  DOI：

  10.1002/1521-3773(20000717)39:14<2470::aid-anie2470>3.0.co;2-r

文献信息

• METHODS AND SYSTEM FOR INTERFERING WITH VIABILITY OF BACTERIA AND RELATED COMPOUNDS AND COMPOSITIONS
  申请人：NEWMAN Dianne K.

  公开号：US20130022578A1

  公开（公告）日：2013-01-24

  Provided herein are methods and systems for interfering with viability of bacteria and related compounds and compositions.

  本文提供了干扰细菌和相关化合物和组合物生存能力的方法和系统。
• Methods and system for interfering with viability of bacteria and related compounds and compositions
  申请人：CALIFORNIA INSTITUTE OF TECHNOLOGY

  公开号：US10689613B2

  公开（公告）日：2020-06-23

  Provided herein are methods and systems for interfering with viability of bacteria and related compounds and compositions.

  本文提供了干扰细菌活力的方法和系统以及相关化合物和组合物。
• Trichothecene-transforming alcohol dehydrogenase, method for transforming trichothecenes and trichothecene-transforming additive
  申请人：Erber Aktiengesellschaft

  公开号：US11001812B2

  公开（公告）日：2021-05-11

  An alcohol dehydrogenase of sequence ID numbers 2, 3 or 4 containing metal ions and a quinone cofactor, or in addition, a functional variant exhibiting a sequence identity of at least 80%, preferably at least 86%, especially preferred at least 89% and at least one redox cofactor for the transformation of at least one trichothecene exhibiting a hydroxyl group on the C-3 atom, as well as a method for the enzymatic transformation of trichothecenes and a trichothecene-transforming additive.

  一种序列 ID 号为 2、3 或 4 的醇脱氢酶，含有金属离子和醌辅助因子，或此外还含有一种功能变体，其序列同一性至少为 80%，优选至少为 86%，特别优选至少为 89%，并含有至少一种氧化还原辅助因子，用于转化至少一种 C-3 原子上带有羟基的单端孢霉烯，以及一种单端孢霉烯酶促转化方法和一种单端孢霉烯转化添加剂。
• Characterization of the Intramolecular Electron Transfer Pathway from 2-Hydroxyphenazine to the Heterodisulfide Reductase fromMethanosarcina thermophila
  作者：Eisuke Murakami、Uwe Deppenmeier、Stephen W. Ragsdale

  DOI：10.1074/jbc.m004809200

  日期：2001.1

  Heterodisulfide reductase (HDR) is a component of the energy-conserving electron transfer system in methanogens, HDR catalyzes the two-electron reduction of coenzyme B-S-S-coenzyme M (CoB-S-S-CoM), the heterodisulfide product of the methyl-CoM reductase reaction, to free thiols, HS-CoB and HS-CoM, HDR from Methanosarcina thermophila contains two b-hemes and two [Fe4S4] clusters. The physiological electron donor for HDR appears to be methanophenazine (MPhen), a membrane-bound cofactor, which can be replaced by a water-soluble analog, 2-hydroxyphenazine (HPhen), This report describes the electron transfer pathway from reduced HPhen (HPhenH(2)) to CoB-S-S-CoM. Steady-state kinetic studies indicate a ping-pong mechanism for heterodisulfide reduction by HPhenH(2) with the following values: k(cat) = 74 s(-1) at 25 degreesC, K-m (HPhenH(2)) = 92 muM, K-m (CoB-S-S-CoM) = 144 muM Rapid freeze-quench EPR and stopped-flow kinetic studies and inhibition experiments using CO and diphenylene iodonium indicate that only the low spin heme and the high potential FeS cluster are involved in CoB-S-S-CoM reduction by HPhenH(2). Fe-S cluster disruption by mersalyl acid inhibits heme reduction by HPhenH(2), suggesting that a 4Fe cluster is the initial electron acceptor from HPhenH(2). We propose the following electron transfer pathway: HPhenH(2) to the high potential 4Fe cluster, to the low potential heme, and finally, to CoB-S-S-CoM.
• Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)
  作者：Reiner HEDDERICH、Albrecht BERKESSEL、Rudolf K. THAUER

  DOI：10.1111/j.1432-1033.1990.tb19331.x

  日期：1990.10

  The reduction of the heterodisulfide of coenzyme M (H‐S‐CoM) and 7‐mercaptoheptanoyl‐l‐threonine phosphate (H‐S‐HTP) is a key reaction in the metabolism of methanogenic bacteria. The heterodisulfide reductase catalyzing this step was purified 80‐fold to apparent homogeneity from Methanobacterium thermoautotrophicum. The native enzyme showed an apparent molecular mass of 550 kDa. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis revealed the presence of three different subunits of apparent molecular masses 80 kDa, 36 kDa, and 21 kDa. The enzyme, which was brownish yellow, contained per mg protein 7 ± 1 nmol FAD, 130 ± 10 nmol non‐heme iron and 130 ± 10 nmol acid‐labile sulfur, corresponding to 4 mol FAD and 72 mol FeS/mol native enzyme. The purified heterodisulfide reductase catalyzed the reduction of CoM‐S‐S‐HTP (app. Km= 0.1 mM) with reduced benzylviologen at a specific rate of 30 μmol · min−1· mg protein−1 (kcat= 68 s−1) and the reduction of methylene blue with H‐S‐CoM (app. Km= 0.2 mM) plus H‐S‐HTP (app. Km < 0.05 mM) at a specific rate of 15 μmol · min−1· mg−1. The enzyme was highly specific for CoM‐S‐S‐HTP and H‐S‐CoM plus H‐S‐HTP. The physiological electron donor/acceptor remains to be identified.