Synthesis and Characterization of High Valnet Reaction Intermediate of Non-Heme Iron Enzymes

非血红素铁酶高效价反应中间体的合成与表征

• 批准号: 14340212
• 负责人: FUJII Hiroshi
• 金额: $ 9.6万
• 依托单位: Okazaki National Research Institutes
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (B)
• 财政年份: 2002
• 资助国家: 日本
• 起止时间: 2002 至 2003
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-14340212/
• 关键词: Bioinorganic Chemistry; Oxygen Activation; Non-Heme Enzyme; High Valnet Iron; Oxidation; Reaction Intermediate; Saren Complex; 酵素活性化; サレン

High-valent iron-oxo species are proposed to be the key reactive intermediate in oxidation reactions catalyzed by both heme and non-heme iron enzymes. In the case of heme enzymes, porphyrin model complexes have been extensively investigated, and oxo-iron (IV) porphyrin π-cation radical have been characterized as the most probable candidate for the active species. However, it is still unclear whether such high-valent iron-oxo species are generated from mononuclear non-heme iron active sites, in which there is no electron pool that can replace the large π-conjugation of the porphyrin ring. It is thus worth challenging to prepare transient oxidizing species from a mononuclear non-heme iron model complex for a detailed study of the electronic structure in comparison with the heme case. To this end, we have prepared a salen iron complex having a mesityl substituent, as a model for mononuclear iron enzymes. We have also tried to make a transient intermediate generated from the sterically hindered salen iron complex and m-chloroperoxybenzoic acid (mCPBA).

高价铁氧化物被认为是血红素和非血红素铁酶催化氧化反应的关键中间体。在血红素酶的情况下，卟啉模型配合物已被广泛研究，氧铁（IV）卟啉π-阳离子自由基已被表征为最有可能的候选活性物种。然而，目前尚不清楚这种高价铁氧是否是由单核非血红素铁活性位点产生的，其中没有可以取代卟啉环大π共轭的电子池。因此，从单核非血红素铁模型络合物中制备瞬时氧化物质，以便与血红素情况进行详细的电子结构研究是值得挑战的。为此，我们制备了一个具有甲酰基取代基的萨伦铁配合物，作为单核铁酶的模型。我们还尝试用位阻萨伦铁配合物和间氯过氧苯甲酸（mCPBA）合成了一种瞬态中间体。

项目成果

Hiroshi Fujii, Yasuhiro Funahashi: "Trigonal Bipyramidal Ferric Aqua Complex with Sterically Hindered Salen Ligand as a Model for Active Site of Protocatechuate 3,4-Dioxygenase"Angew. Chemie. Int. Ed.. 41. 3638-3641 (2002)

Hiroshi Fujii、Yasuhiro Funahashi：“具有空间位阻 Salen 配体的三角双锥铁水复合物作为原儿茶酸 3,4-双加氧酶活性位点的模型”Angew。

Hiroshi Fujii et al.: "Essential Amino Acid Residues Controlling the Unique Regioselectivity of Heme Oxygenase in Psudomonas aeruginosa"J.Am.Chem.Soc.. 126(印刷中). (2004)

Hiroshi Fujii 等人：“控制铜绿假单胞菌中血红素加氧酶的独特区域选择性的必需氨基酸残基”J.Am.Chem.Soc. 126（印刷中）。

Masataka Ohashi et al.: "Preparation of Artificial Metalloenzymes by Insertion of Chromium(iii) Schiff Base Complexes into Apomyoglobin Mutants"Angew.Chemie.Int.Ed.. 42. 7418-7426 (2003)

Masataka Ohashi 等人：“通过将铬(iii)席夫碱配合物插入脱肌红蛋白突变体中制备人工金属酶”Angew.Chemie.Int.Ed..42.7418-7426(2003)

Xuhong Zhang et al.: "Regiospecificity of Each of the Three Steps of Heme Oxygenase Reaction from Hemin to meso-Hydroxyhemin, from meso-Hydroxyhemin to Verdoheme, and from Verdoheme to Biliverdin"Biochemistry. 42. 7418-7426 (2003)

Xuhong Zhang等人：“从血红素到内消旋羟基血红素，从内消旋羟基血红素到维多血红素，以及从维多血红素到胆绿素的血红素加氧酶反应三个步骤中每一步的区域特异性”生物化学。

Roman Davydov et al.: "Kinetic Isotope Effects on the Rate-Limiting Step of Heme Oxygenase Catalysis Indicate Concerted Proton Transfer/Heme Hydroxylation"J.Am.Chem.Soc.. 125. 16208-16209 (2003)

Roman Davydov 等人：“动力学同位素对血红素加氧酶催化限速步骤的影响表明协同质子转移/血红素羟基化”J.Am.Chem.Soc.. 125. 16208-16209 (2003)