Dihydromethanophenazine

• 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: Dihydromethanophenazine
• 英文别名: 2-[(6E,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraenoxy]-5,10-dihydrophenazine
• 化学式: C₃₇H₅₂N₂O
• 分子量: 540.8
• InChiKey: LNCNNIYZOUNGMU-QAAQOENVSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  12.2
• 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：
  33.3
• 氢给体数：
  2
• 氢受体数：
  3

反应信息

• 作为产物：
  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

文献信息

• Isolation and Characterization of Methanophenazine and Function of Phenazines in Membrane-Bound Electron Transport of<i>Methanosarcina mazei</i>Gö1
  作者：Hans-Jörg Abken、Mario Tietze、Jens Brodersen、Sebastian Bäumer、Uwe Beifuss、Uwe Deppenmeier

  DOI：10.1128/jb.180.8.2027-2032.1998

  日期：1998.4.15

  A hydrophobic, redox-active component with a molecular mass of 538 Da was isolated from lyophilized membranes ofMethanosarcina mazeiGö1 by extraction with isooctane. After purification on a high-performance liquid chromatography column, the chemical structure was analyzed by mass spectroscopy and nuclear magnetic resonance studies. The component was called methanophenazine and represents a 2-hydroxyphenazine derivative which is connected via an ether bridge to a polyisoprenoid side chain. Since methanophenazine was almost insoluble in aqueous buffers, water-soluble phenazine derivatives were tested for their ability to interact with membrane-bound enzymes involved in electron transport and energy conservation. The purified F₄₂₀H₂dehydrogenase fromM. mazeiGö1 showed highest activity with 2-hydroxyphenazine and 2-bromophenazine as electron acceptors when F₄₂₀H₂was added. Phenazine-1-carboxylic acid and phenazine proved to be less effective. TheK_mvalues for 2-hydroxyphenazine and phenazine were 35 and 250 μM, respectively. 2-Hydroxyphenazine was also reduced by molecular hydrogen catalyzed by an F₄₂₀-nonreactive hydrogenase which is present in washed membrane preparations. Furthermore, the membrane-bound heterodisulfide reductase was able to use reduced 2-hydroxyphenazine as an electron donor for the reduction of CoB-S-S-CoM. Considering all these results, it is reasonable to assume that methanophenazine plays an important role in vivo in membrane-bound electron transport ofM. mazeiGö1.

  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。
• 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.
• Purification and Properties of the Heme- and Iron−Sulfur-Containing Heterodisulfide Reductase from <i>Methanosarcina thermophila</i>
  作者：Mihaela Simianu、Eisuke Murakami、John M. Brewer、Stephen W. Ragsdale

  DOI：10.1021/bi9726483

  日期：1998.7.1

  The heterodisulfide reductase (HDR) from Methanosarcina thermophila was purified to homogeneity from acetate-grown cells. In the absence of detergents, HDR consisted of an eight-protein complex with hydrogenase activity. However, when HDR was purified in the presence of 0.6% Triton X-100, a two-subunit (53 and 27 kDa) high specific activity (similar to 200 units mg(-1)) enzyme was obtained that lacked hydrogenase activity. Sedimentation equilibrium experiments demonstrated that HDR has a molecular mass of 206 kDa and a high partial specific volume (0.9 cm(3)/g), indicating that the purified protein contains a significant amount of bound lipid. Like the HDR from Methanosarcina barkeri [Kunkel, A., Vaupel, M., Helm, S., Thauer, R. K., and Hedderich, R. (1997) Eur. J. Biochem. 244, 226-234], it was found to contain two discrete b-type hemes in the small subunit and two distinct [Fe4S4](2+/1+) clusters in the large subunit. One heme is high-spin and has a high midpoint potential (-23 mV), whereas the other heme apparently is low-spin and exhibits a relatively low midpoint potential (-180 mV). Only the high-spin heme binds CO. The midpoint potentials for the two clusters are -100 and -400 mV. In the fully reduced state, a complicated EPR spectrum with g values of 2.03, 1.97, 1.92, and 1.88 was observed. This spectrum resembles that of 8Fe ferredoxins in the fully reduced state, indicating that the two clusters in HDR are near enough to experience relatively strong dipolar interactions. Kinetic studies in which CO oxidation is coupled to heterodisulfide reduction strongly indicate that a membrane-associated compound is the direct electron donor to HDR. An electron-transfer pathway is presented that postulates a mechanism for coupling electron transport to proton translocation.