Adrenodoxin is an iron-sulfur protein that belongs to the broad family of the [2Fe-2S]-type ferredoxins found in plants, animals and bacteria. Its primary function as a soluble electron carrier between the NADPH-dependent adrenodoxin reductase and several cytochromes P450 makes it an irreplaceable component of the steroid hormones biosynthesis in the adrenal mitochondria of vertebrates. This review intends to summarize current knowledge about structure, function, and biochemical behavior of this electron transferring protein. We discuss the recently solved first crystal structure of the vertebrate-type ferredoxin, the truncated adrenodoxin Adx(4-108), that offers the unique opportunity for better understanding of the structure-function relationships and stabilization of this protein, as well as of the molecular architecture of [2Fe-2S] ferredoxins in general. The aim of this review is also to discuss molecular requirements for the formation of the electron transfer complex. Essential comparison between bacterial putidaredoxin and mammalian adrenodoxin will be provided. These proteins have similar tertiary structure, but show remarkable specificity for interactions only with their own cognate cytochrome P450. The discussion will be largely centered on the protein-protein recognition and kinetics of adrenodoxin dependent reactions.

中文翻译：

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肾上腺毒素：结构，稳定性和电子转移性质。

肾上腺毒素是一种铁硫蛋白，属于在植物，动物和细菌中发现的[2Fe-2S]型铁氧还蛋白的广泛家族。它的主要功能是作为NADPH依赖性肾上腺素还原酶和几种细胞色素P450之间的可溶性电子载体，使其成为脊椎动物肾上腺线粒体中类固醇激素生物合成的不可替代的成分。这篇综述旨在总结有关该电子转移蛋白的结构，功能和生化行为的当前知识。我们讨论了最近解决的脊椎动物型铁氧还蛋白的第一个晶体结构，即截短的肾上腺素Adx（4-108），它为更好地了解该蛋白的结构-功能关系和稳定性提供了独特的机会，以及[2Fe-2S]铁氧还蛋白的分子结构。这篇综述的目的还在于讨论形成电子转移配合物的分子要求。将提供细菌普达氧还蛋白和哺乳动物肾上腺毒素之间的基本比较。这些蛋白质具有相似的三级结构，但仅与它们自己的同源细胞色素P450相互作用时显示出显着的特异性。讨论将主要集中在对肾上腺毒素依赖性反应的蛋白质-蛋白质识别和动力学上。但仅与它们自己的同源细胞色素P450相互作用时显示出显着的特异性。讨论将主要集中在对肾上腺毒素依赖性反应的蛋白质-蛋白质识别和动力学上。但仅与它们自己的同源细胞色素P450相互作用时显示出显着的特异性。讨论将主要集中在对肾上腺毒素依赖性反应的蛋白质-蛋白质识别和动力学上。