首页> 外文期刊>Journal of biological inorganic chemistry: JBIC: a publication of the Society of Biological Inorganic Chemistry >Metalloproteins: structure and function-X-ray crystallographic structure analyses and characterization of a blue copper protein, pseudoazurin, Met16Ile variant
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Metalloproteins: structure and function-X-ray crystallographic structure analyses and characterization of a blue copper protein, pseudoazurin, Met16Ile variant

机译:金属蛋白:结构和功能-X射线晶体学分析和表征蓝色铜蛋白,假天青素,Met16Ile变体

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摘要

Pseudoazurin (PAz) from Achromobacter cycloclastes functions as an electron donor to nitrite reductase and nitrous oxide reductase. The copper atom is coordinated by His40 and His81 imidazole N atoms of, Cys78 thiolate S atom, and Met86 sulfide S atom with distorted tetrahedral geometry. The Met16 residue is located in the vicinity of His81 and weakly interacted to the active site [1], and several Met16 mutated PAz were studied to shed light on the role of weak interaction on the electronic structure of blue copper protein.
机译:环色无色杆菌中的伪天青素(PAz)充当亚硝酸还原酶和一氧化二氮还原酶的电子供体。铜原子由具有扭曲的四面体几何形状的His40和His81咪唑N原子,Cys78硫醇盐S原子和Met86硫化物S原子配位。 Met16残基位于His81附近并与活性位点弱相互作用[1],并研究了多个Met16突变的PAz揭示了弱相互作用对蓝铜蛋白电子结构的作用。

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