Structural biology of copper trafficking.
Structural biology of copper trafficking.
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DOI：
10.1021/cr900104z
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发表时间：
2009-10
期刊：
影响因子：
62.1
通讯作者：
Rosenzweig, Amy C.
中科院分区：
文献类型：
--
作者：
Boal, Amie K.;Rosenzweig, Amy C.
1.1 背景铜在生物系统中的使用与大约 17 亿年前氧气气氛的出现同时发生。 O 2 的存在既使不溶性 Cu (I) 氧化为更易溶解且生物可利用的 Cu (II)，又导致需要电位在 0− 800 mV 范围内的氧化还原活性金属。铜不仅满足了这一需求，而且将 Fe (II) 氧化为不溶性 Fe (III) 形式使得铁的使用更加昂贵。(1-5) 因此，铜在许多与 O 2 反应的蛋白质中发挥着关键作用。通常，O 2 反应中心是单核（2 型）、双核（3 型）或三核（2 型和 3 型）。经过充分研究的单核铜酶包括单加氧酶多巴胺-β-羟化酶和肽基甘氨酸 α-羟基化单加氧酶以及还含有有机辅因子的氧化酶，例如胺、半乳糖和赖氨酰氧化酶。(6) 双核铜蛋白包括 O 2 载体血蓝蛋白和酶，例如酪氨酸酶和儿茶酚氧化酶。(7) 铜在许多电子传递蛋白中也发挥着关键作用。单核 1 型（蓝铜）中心存在于质体蓝素和天青蛋白等蛋白质中。(8) 漆酶、抗坏血酸氧化酶和铜蓝蛋白等多铜氧化酶含有催化三核 2 型/3 型位点和电子转移 1 型位点。(9, 10) 铜中心的类型分类源自光学和电子顺磁共振 (EPR) 光谱特性，还有一些值得注意的例外，包括细胞色素 c 氧化酶 (11) 和一氧化二氮还原酶中的半胱氨酸桥双核 Cu A 电子转移位点、一氧化二氮还原酶中的四核催化 Cu Z 中心 (12) 以及颗粒甲烷单加氧酶中拟议的催化铜中心。 (13-15)
1.1 BackgroundThe use of copper in biological systems coincides with the advent of an oxygen atmosphere about 1.7 billion years ago. The presence of O 2 both allowed the oxidation of insoluble Cu (I) to the more soluble and bioavailable Cu (II) and led to the requirement for a redox active metal with potentials in the 0− 800 mV range. Not only did copper meet this need, but the oxidation of Fe (II) to the insoluble Fe (III) form rendered the use of iron more energetically expensive.(1-5) As a result, copper plays a key role in many proteins that react with O 2. Generally, O 2-reactive centers are mononuclear (type 2), dinuclear (type 3), or trinuclear (type 2 and type 3). Well studied mononuclear copper enzymes include the monooxygenases dopamine-β-hydroxylase and peptidylglycine α-hydroxylating monooxygenase as well as oxidases that also contain organic cofactors, such as amine, galactose, and lysyl oxidases.(6) Dinuclear copper proteins include the O 2 carrier hemocyanin and enzymes such as tyrosinase and catechol oxidase.(7) Copper also plays a key role in numerous electron transfer proteins. Mononuclear type 1 (blue copper) centers are found in proteins such as plastocyanin and azurin.(8) The multicopper oxidases such as laccase, ascorbate oxidase, and ceruloplasmin contain both a catalytic trinuclear type 2/type 3 site and an electron transfer type 1 site.(9, 10) The classification of copper centers into types is derived from optical and electron paramagnetic resonance (EPR) spectroscopic properties, and there are some notable exceptions, including the cysteine-bridged dinuclear Cu A electron transfer site in cytochrome c oxidase (11) and nitrous oxide reductase, the tetranuclear catalytic Cu Z center in nitrous oxide reductase,(12) and the proposed catalytic copper center in particulate methane monooxygenase.(13-15)
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影响因子：
5.4
作者：
Banci, L;Bertini, I;Rosato, A
通讯作者：
Rosato, A
影响因子：
7
作者：
Arnesano, F;Banci, L;O'Halloran, TV
通讯作者：
O'Halloran, TV
DOI：
10.1073/pnas.0504472103
发表时间：
2006-04-11
影响因子：
11.1
作者：
Achila, D;Banci, L;Huffman, DL
通讯作者：
Huffman, DL
影响因子：
2.9
作者：
Anastassopoulou, I;Banci, L;Rosato, A
通讯作者：
Rosato, A
影响因子：
2.9
作者：
Banci, L;Bertini, I;Del Conte, R
通讯作者：
Del Conte, R