基于肌红蛋白的氧激活蛋白的理性设计

金属酶催化了生命活动及工业催化中的很多重要反应。天然金属酶的研究往往受限于蛋白质本身结构复杂、表达纯化困难等问题。通过理性设计,可以在分子量小、结构简单、易于表达的骨架蛋白中模拟天然金属酶的结构、光谱和功能,构建人工金属酶。人工酶可以为天然酶的机制研究提供新的平台。本文中,笔者探讨以肌红蛋白为骨架蛋白,通过结构特征的模拟、非天然氨基酸的引入等手段,模拟氧激活蛋白,尤其是氧化酶。综述以对理性设计得到的人工氧化酶的反应中间体进行研究的进展,发现金属酶活性中心的酪氨酸作为催化反应的关键残基,对于氧化反应的调控非常重要; 而在小分子量骨架蛋白中模拟天然金属酶是一种人工金属酶分子设计的方法,可以用于研究血红素酶外的其他金属酶。

Expansion of Redox Chemistry in Designer Metalloenzymes

Artificial Metalloenzyme Design with Unnatural Amino Acids and Non-Native Cofactors

A genetically engineered Escherichia coli that senses and degrades tetracycline antibiotic residue

Engineering the metal-binding loop at a type 1 copper center by circular permutation

Circular permutation of the cupredoxin azurin creates a break on the metal binding loop, highlighting the loop's flexibility.

Improving artificial metalloenzymes' activity by optimizing electron transfer

This feature article discusses the strategies to optimize electron transfer efficiency, towards enhancing the activity of artificial metalloenzymes.

Effect of circular permutation on the structure and function of type 1 blue copper center in azurin

Biosynthetic approach to modeling and understanding metalloproteins using unnatural amino acids

Ultrafast Photoinduced Electron Transfer in Green Fluorescent Protein Bearing a Genetically Encoded Electron Acceptor

Significant improvement of oxidase activity through the genetic incorporation of a redox-active unnatural amino acid

Incorporation of 3-methoxytyrosine boosts the oxidase activity of the myoglobin model of oxidase, stressing the importance of the redox potential tuning of tyrosine.

Defining the Role of Tyrosine and Rational Tuning of Oxidase Activity by Genetic Incorporation of Unnatural Tyrosine Analogs

A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme

Direct EPR Observation of a Tyrosyl Radical in a Functional Oxidase Model in Myoglobin during both H2O2and O2Reactions

Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers

Significant Enhancement of hPrx1 Chaperone Activity through Lysine Acetylation

Significant Increase of Oxidase Activity through the Genetic Incorporation of a Tyrosine-Histidine Cross-Link in a Myoglobin Model of Heme-Copper Oxidase