reductase from Pseudomonas species NCIB 9816-4

• 英文名称: reductase from Pseudomonas species NCIB 9816-4

反应信息

• 作为试剂：
  描述：

  双环[4.1.0]庚烷 在 lignostilbene alphabeta-dioxygenase 、 reductase from Pseudomonas species NCIB 9816-4 air 、 1,4-dihydronicotinamide adenine dinucleotide 、 Fe₂S₂ ferredoxin from Pseudomonas species NCIB 9816-4 作用下， 以 水 为溶剂， 反应 0.5h， 以61.8%的产率得到2-环己烯-1-甲醇
  参考文献：
  名称：

  Radical Intermediates in Monooxygenase Reactions of Rieske Dioxygenases

  摘要：

  Rieske dioxygenases catalyze the cis-dihydroxylation of a wide range of aromatic compounds to initiate their biodegradation. The archetypal Rieske dioxygenase naphthalene 1,2-dioxygenase (NDOS) catalyzes dioxygenation of naphthalene to form (+)-cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene. NDOS is composed of three proteins: a reductase, a ferredoxin, and an alpha(3)beta(3) oxygenase (NDO). In each alpha subunit, NDO contains a Rieske Fe2S2 cluster and a mononuclear iron site where substrate dihydroxylation occurs. NDOS also catalyzes monooxygenase reactions for many substrates. The mechanism of the reaction is unknown for either the mono- or dioxygenase reactions but has been postulated to involve direct reaction of either a structurally characterized Fe(III)-hydroperoxy intermediate or the electronically equivalent Fe(V)-oxo-hydroxo intermediate formed by O-O bond cleavage before reaction with substrate. The reaction for the former intermediate is expected to proceed through cationic intermediates, while the latter is anticipated to initially form a radical intermediate. Here the monooxygenation reactions of the diagnostic probe molecules, norcarane and bicyclohexane, are investigated. In each case, a significant amount of the rearrangement product derived from a radical intermediate (lifetime of 11-18 ns) is observed, while little or no ring expansion product from a cationic intermediate is formed. Thus, monooxygenation of these molecules appears to proceed via the Fe(V)-oxo-hydroxo intermediate. The formation of this high-valent intermediate shows that it must also be considered as a possible participant in the dioxygenation reaction, in contrast to computational studies but in accord with previous biomimetic studies.

  DOI：

  10.1021/ja068188v