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首页> 外文期刊>Biochemistry >Transient Potein Interactions Studied by NMR Spectroscopy: The Case of Cytochrome c and Adrenodoxin
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Transient Potein Interactions Studied by NMR Spectroscopy: The Case of Cytochrome c and Adrenodoxin

机译：核磁共振波谱研究瞬态波坦相互作用：细胞色素c和肾上腺素的情况。

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The interaction between yeast iso-1-cytochrome c (C102T) and two forms of bovine adrenodoxin, the wild type and a truncated form comprising residues 4-108, has been investigated using a combination of one- and two-dimensional heteronuclear NMR spectroscopy. Chemical shift perturbations and line broadening of amide resonances in the [~(15)N, ~1H]HSQC spectrum for both ~(15)N-labeled cytochrome c and adrenodoxin in the presence of the unlabeled partner protein indicate the formation of a transient complex, with a K_a of (4+-1)X10~4 M~(-1) and a lifetime of <3 ms. The perturbed residues map over a large surface area for both proteins. For cytochrome c, the dominating effects are located around the exposed heme edge but with other areas also affected upon formation of the complex. In the case of adrenodoxin, effects are seen in both the recognition and core domains, with the largest perturbations in the recognition domain. These results indicate that the complex has a dynamic nature, with delocalized binding of cytochrome c on adrenodoxin. A comparison with other transient complexes of redox proteins places this complex between well-defined complexes such as the cytochrome c-cytochrome c peroxidase complex and entirely dynamic complexes such as the cytochrome b_5-myoglobin complex.
机译：已使用一维和二维异核NMR光谱技术研究了酵母异-1-细胞色素c（C102T）与两种形式的牛肾上腺毒素之间的相互作用，即野生型和包含残基4-108的截短形式。在未标记的伴侣蛋白存在下，〜（15）N标记的细胞色素c和肾上腺素毒素的[〜（15）N，〜1H] HSQC光谱中的化学位移扰动和酰胺共振的谱线展宽。 K_a为（4 + -1）X10〜4 M〜（-1），寿命<3 ms。被干扰的残基在两种蛋白质的较大表面积上均作图。对于细胞色素c，主要作用位于暴露的血红素边缘周围，但其他区域也受复合物形成的影响。在肾上腺毒素的情况下，在识别域和核心域中都可以看到作用，在识别域中的干扰最大。这些结果表明该复合物具有动态性质，细胞色素c在肾上腺毒素上的结合是非定域的。与氧化还原蛋白的其他瞬时复合物的比较将这种复合物置于定义明确的复合物（例如细胞色素c-细胞色素c过氧化物酶复合物）和完全动态的复合物（例如细胞色素b_5-肌红蛋白复合物）之间。

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