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小云云。新蟲(chóng) (小有名氣)
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[求助]
求大神幫忙把下面兩段的文獻(xiàn)摘要翻譯成中文。。。
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1 A single mutation within a flavoprotein is capable of switching the catalytic activity of a dehalogenase into a nitroreductase. This change in function correlates with a destabilization of the one-electron-reduced flavin semiquinone that is differentially expressed in the nitro-FMN reductase superfamily during redox cycling. The diversity of function within such a superfamily therefore has the potential to arise from rapid evolution, and its members should provide a convenient basis for developing new catalysts with an altered specificity of choice. 2 The coordination bond between gold and sulfur (Au–S) has been widely studied and utilized in many fields. However, detailed investigations on the basic nature of this bond are still lacking. A gold-specific binding protein, GolB, was recently identified, providing a unique opportunity for the study of the Au–S bond at the molecular level. We probed the mechanical strength of the gold–sulfur bond in GolB using single-molecule force spectroscopy. We measured the rupture force of the Au–S bond to be 165 pN, much lower than Au–S bonds measured on different gold surfaces (∼1000 pN). We further solved the structures of apo-GolB and Au(I)–GolB complex using X-ray crystallography. These structures showed that the average Au–S bond length in GolB is much longer than the reported average value of Au–S bonds. Our results highlight the dramatic influence of the unique biological environment on the stability and strength of metal coordination bonds in proteins. |
金蟲(chóng) (正式寫(xiě)手)
| 金硫配位鍵已在眾多領(lǐng)域得到了廣泛研究及應(yīng)用,但對(duì)于該鍵的基礎(chǔ)性質(zhì)還有待研究。近來(lái),一種含有特定金建的蛋白質(zhì)GolB已被確定,這為在分子水平上研究金-硫鍵提供了獨(dú)特的條件。我們用單分子力光譜檢測(cè)了GOlB中金-硫鍵的機(jī)械強(qiáng)度。該金-硫鍵的斷裂力為165pN,遠(yuǎn)小于不同金原子表面的金-硫鍵(約1000pN).我們進(jìn)一步用x射線結(jié)晶法確定了apo-GolB and Au(I)–GolB復(fù)合物的結(jié)構(gòu),結(jié)果表明GolB中金-硫鍵的平均鍵長(zhǎng)遠(yuǎn)大于所報(bào)道的值。研究結(jié)果強(qiáng)調(diào)了獨(dú)特的生物環(huán)境對(duì)蛋白質(zhì)中金屬配位鍵的穩(wěn)定性和強(qiáng)度的顯著影響 我是外行,僅供參考 |
新蟲(chóng) (小有名氣)
鐵桿木蟲(chóng) (正式寫(xiě)手)
| 黃素蛋白中的單個(gè)氨基酸殘基的突變就可能引起它的催化活性改變——從脫鹵酶變成硝基還原酶。黃素蛋白功能上的轉(zhuǎn)化可能與黃素醌上的還原性電子的激發(fā)有關(guān)。這與在電子傳遞鏈中nitro-FMN還原酶的電子激發(fā)有所不同。黃素蛋白超家族的功能具有多樣性,這可能是跳躍性進(jìn)化的結(jié)果。研究人員通過(guò)改變這個(gè)超家族的成員酶的某個(gè)氨基酸殘基來(lái)研發(fā)新的催化劑。 |
新蟲(chóng) (小有名氣)
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