2-(2'-hydroxy)biphenyl benzene sulfinate

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: 2-(2'-hydroxy)biphenyl benzene sulfinate
• 英文别名: 2-(2-Sulfinophenyl)phenolate；2-(2-sulfinophenyl)phenolate
• 化学式: C₁₂H₉O₃S
• 分子量: 233.268
• InChiKey: HPKSNFTYZHYEKV-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  1.8
• 重原子数：
  16
• 可旋转键数：
  1
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  79.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-(2'-hydroxy)biphenyl benzene sulfinate 、 水 生成 邻苯基苯酚 、 氢(+1)阳离子 、 三氧化硫
  参考文献：
  名称：

  A novel enzyme, 2′-hydroxybiphenyl-2-sulfinate desulfinase (DszB), from a dibenzothiophene-desulfurizing bacterium Rhodococcus erythropolis KA2-5-1: gene overexpression and enzyme characterization

  摘要：

  Dibenzothiophene (DBT), a model of organic sulfur compound in petroleum, is microbially desulfurized to 2-hydroxybiphenyl (2-HBP), and the gene operon dszABC was required for DBT desulfurization. The final step in the microbial DBT desulfurization is the conversion of 2'-hydroxybiphenyl-2-sulfinate (HBPSi) to 2-HBP catalyzed by DszB. In this study, DszB of a DBT-desulfurizing bacterium Rhodococcus erythropolis KA2-5-1 was overproduced in Escherichia coli by coexpression with chaperonin genes, groEL/groES, at 25 degreesC. The recombinant DszB was purified to homogeneity and characterized. The optimal temperature and pH for DszB activity were 35 degreesC and about 7.5, respectively. The K-m and k(cat) values for HBPSi were 8.2 muM and 0.123.s(-1), respectively. DszB has only one cysteine residue, and the mutant enzyme completely lost the activity when the cysteine residue was changed to a serine residue. This result together with experiments using inhibitors showed that the cysteine residue contributes to the enzyme activity. DszB was also inhibited by a reaction product, 2-HBP (K-i = 0.25 mM), and its derivatives, but not by the other reaction product, sulfite. The enzyme showed it narrow substrate specificity: only 2-phenylbenzene sulfinate except HBPSi served as a substrate among the aromatic and aliphatic sulfinates or sulfonates tested. DszB was thought to be a novel enzyme (HBPSi desulfinase) in that it could specifically cleave the carbon-sulfur bond of HBPSi to give 2-HBP and sulfite ion without the aid of any other proteinic components and coenzymes. (C) 2002 Published by Elsevier Science B.V.

  DOI：

  10.1016/s0167-4838(02)00365-5
• 作为产物：
  描述：

  二苯并噻吩 在 pRKPBP 、 Rhodococcus erythropolis KA₂-5-1 作用下， 以 phosphate buffer 为溶剂， 反应 1.0h， 生成 邻苯基苯酚 、 2-(2'-hydroxy)biphenyl benzene sulfinate
  参考文献：
  名称：

  Improvememt of Desulfurization Activity in Rhodococcus erythropolis KA2-5-1 by Genetic Engineering

  摘要：

  Rhodococus erythropolis KA2-5-1 能将二苯并噻吩（DBT）脱硫成 2-羟基联苯。将源自红球菌 IFO3338 的隐性质粒 pRC4 与大肠杆菌载体结合，构建了大肠杆菌-红球菌穿梭载体。对 2582-bp pRC4 的完整核苷酸序列进行了分析。根据其推定复制基因的特征，pRC4 被归入 pAL5000 相关复制子家族。从 KA2-5-1 克隆的脱硫基因簇 dszABC 和相关的还原酶基因 dszD 被重新导入 KA2-5-1 并高效表达。载体上携带两个dszABC簇和一个dszD的转化子的DBT脱硫能力比亲本菌株高出约4倍，转化子对轻质油（LGO）的脱硫活性也有所提高。用气相色谱-原子发射检测法分析了反应前后 LGO 中的硫成分。

  DOI：

  10.1271/bbb.65.239

文献信息

• Dibenzothiophene Catabolism Proceeds via a Flavin-N5-oxide Intermediate
  作者：Sanjoy Adak、Tadhg P. Begley

  DOI：10.1021/jacs.6b00583

  日期：2016.5.25

  The dibenzothiophene catabolic pathway converts dibenzothiophene to 2-hydroxybiphenyl and sulfite. The third step of the pathway, involving the conversion of dibenzothiophene sulfone to 2-(2-hydroxyphenyl)-benzenesulfinic acid, is catalyzed by a unique flavoenzyme DszA. Mechanistic studies on this reaction suggest that the C2 hydroperoxide of dibenzothiophene sulfone reacts with flavin to form a flavin-N5-oxide

  二苯并噻吩分解代谢途径将二苯并噻吩转化为 2-羟基联苯和亚硫酸盐。该途径的第三步涉及将二苯并噻吩砜转化为 2-(2-羟基苯基)-苯亚磺酸，由独特的黄素酶 DszA 催化。该反应的机理研究表明二苯并噻吩砜的C2氢过氧化物与黄素反应形成黄素-N5-氧化物。通过 LC-MS 分析、化学合成的 FMN-N5-氧化物和 (18)O2 标记研究的共洗脱实验，证实了黄素-N5-氧化物的中间作用。
• Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases
  作者：Arne Matthews、Raspudin Saleem-Batcha、Jacob N. Sanders、Frederick Stull、K. N. Houk、Robin Teufel

  DOI：10.1038/s41589-020-0476-2

  日期：2020.5

  motif for dioxygen activation and N5-functionalization, suggesting a conserved pathway that may be operative in numerous characterized and uncharacterized flavoenzymes from diverse organisms. Our findings show that overlooked flavin-N5-oxygen adducts are more widespread and may facilitate versatile chemistry, thus upending the notion that flavin monooxygenases exclusively function as nature’s equivalents

  黄素依赖性酶催化的标志性反应之一是将衍生自分子氧的氧原子结合到有机底物中。几十年来，这些黄素单加氧酶被认为只使用黄素-C4a-(氢)过氧化物作为它们的氧转移中间体。我们证明了黄素酶可以替代使用黄素-N5-过氧化物作为催化的软α-亲核试剂，这使得经典单加氧酶无法获得化学。这包括，例如，碳杂键的氧化还原中性裂解或惰性环境污染物通过非典型氧化作用的脱卤。我们进一步确定了分子氧激活和 N5 功能化的共享结构基序，表明可能在来自不同生物的许多特征和未特征的黄素酶中起作用的保守途径。我们的研究结果表明，被忽视的黄素-N5-氧加合物更为普遍，并可能促进多功能化学，从而颠覆了黄素单加氧酶在合成化学中仅作为有机过氧化物的天然等效物的观点。
• Purification and characterization of dibenzothiophene (DBT) sulfone monooxygenase, an enzyme involved in DBT desulfurization, from Rhodococcus erythropolis D-1
  作者：Takashi Ohshiro、Tatsuya Kojima、Kuniaki Torii、Hiroshi Kawasoe、Yoshikazu Izumi

  DOI：10.1016/s1389-1723(00)87088-7

  日期：——

  The optimal temperature and pH for DszA activity were 35 degrees C and about 7.5. The activity of the enzyme was inhibited by Mn2+, Ni2+, 2,2'-bipyridine, and 8-quinolinol, suggesting that a metal might be involved in its activity. DszA acted on not only DBT sulfone but also on dibenz[c,e][1,2]oxathiin 6-oxide and dibenz[c,e][1,2]oxathiin 6,6-dioxide. Dihydroxybiphenyl was formed from the latter two

  二苯并噻吩（DBT）是石油中的有机硫化合物的模型，被红球菌D-1微生物脱硫成2-羟基联苯。硫特异性DBT脱硫涉及三种脱硫（Dsz）酶-DszC，A和B-和黄素还原酶。在这项研究中，DszA是从R. erythropolis D-1中纯化，鉴定和结晶的。DszA，DBT砜单加氧酶，是微生物DBT脱硫代谢中的第二种酶，在黄素还原酶存在的情况下催化DBT砜向2'-羟基联苯2-亚磺酸的转化，并裂解DBT骨架中的碳-硫键。使用阴离子交换柱色谱分离负责DBT脱硫的四个酶馏分，然后将DszA纯化至均质。一周之内观察到DszA的多边形晶体。发现DszA具有97kDa的分子量并且由具有50kDa的相同质量的两个亚基组成。纯化的DszA的N末端氨基酸序列与R. erythropolis IGTS8的dszA的推导氨基酸序列完全重合，除了后者N末端的蛋氨酸残基。DszA活性的最佳温度和pH为35℃和约7.5。该酶的活性受到Mn2
• Molecular mechanisms of biocatalytic desulfurization of fossil fuels
  作者：Kevin A. Gray、Olga S. Pogrebinsky、Gregory T. Mrachko、Lei Xi、Daniel J. Monticello、Charles H. Squires

  DOI：10.1038/nbt1296-1705

  日期：1996.12

  The development of biocatalytic desulfurization of petroleum fractions may allow its use in place of conventional hydrodesulfurization (HDS). Dibenzothiophene (DBT) is representative of a broad range of sulfur heterocycles found in petroleum that are recalcitrant to desulfurization via HDS. Rhodococcus sp. strain IGTS8 has the ability to convert DBT to 2-hydroxybiphenyl (HBP) with the release of inorganic sulfur. The conversion of DBT to HBP is catalyzed by a multienzyme pathway consisting of two mono-oxygenases and a desulfinase. The final reaction catalyzed by the desulfinase appears to be the rate limiting step in the pathway. Each of the enzymes has been purified to homogeneity and their kinetic and physical properties studied. Neither monooxygenase has a tightly bound cofactor and each requires an NADH-FMN oxidoreductase for activity. An NADH-FMN oxidoreductase has been purified from Rhodococcus and is a protein of approximately 25,000 molecular weight with no apparent sequence homology to any other protein in the databases. We describe a unique sulfur acquisition system that Rhodococcus uses to obtain sulfur from very stable heterocyclic molecules.

  石油馏分生物催化脱硫技术的发展可能会使其取代传统的加氢脱硫（HDS）技术。二苯并噻吩（DBT）是石油中广泛存在的硫杂环的代表，这些杂环对通过加氢脱硫法进行脱硫具有顽固性。Rhodococcus sp. 菌株 IGTS8 能够将 DBT 转化为 2-hydroxybiphenyl (HBP)，并释放出无机硫。DBT 向 HBP 的转化是由两个单氧化酶和一个脱硫酶组成的多酶途径催化的。脱硫酶催化的最终反应似乎是该途径中的限速步骤。每种酶都已纯化至均一，并对其动力学和物理性质进行了研究。这两种单加氧酶都没有紧密结合的辅助因子，都需要 NADH-FMN 氧化还原酶才能发挥作用。从 Rhodococcus 中纯化出了一种 NADH-FMN 氧化还原酶，它是一种分子量约为 25,000 的蛋白质，与数据库中的任何其他蛋白质都没有明显的序列同源性。我们描述了 Rhodococcus 从非常稳定的杂环分子中获取硫的独特硫获取系统。
• Flavin-N5-oxide: A new, catalytic motif in flavoenzymology
  作者：Sanjoy Adak、Tadhg P. Begley

  DOI：10.1016/j.abb.2017.08.001

  日期：2017.10

  Flavin-N5-oxide is a recently discovered intermediate used by EncM (1,3-diketone oxidation), DszA (sulfone monooxygenase) and RutA (amide monooxygenase). This review describes the mechanism of these enzymes and proposes criteria for the identification of additional Flavin-N5-oxide dependent enzymes. (C) 2017 Elsevier Inc. All rights reserved.