EFFECT OF PEGYLATION ON THE STRUCTURE AND FUNCTION OF HORSE CYTOCHROME-C
EFFECT OF PEGYLATION ON THE STRUCTURE AND FUNCTION OF HORSE CYTOCHROME-C
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DOI：
10.1021/bc00027a008
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发表时间：
1994-05-01
影响因子：
4.7
通讯作者：
MABROUK, PA
中科院分区：
文献类型：
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作者：
MABROUK, PA
描述了不同修饰程度 (n(av) = 6, 19) 的聚乙二醇 (PEG; av FW 5000) 修饰的马细胞色素 c (cyt c(PEG)n)（Fe2+ 和 Fe3+ 形式）的制备和分光光度表征，包括紫外-可见光谱、圆二色光谱、共振拉曼光谱和循环伏安法。 Fe2+ 和 Fe3+ 形式的 UV-vis 和圆二色性光谱特征的主要光谱变化证明了 cyt c 的广泛修饰 (n(av) = 19) 导致血红素的总体结构变形。然而，通过六个 PEG 残基对细胞色素 c 进行修饰，产生一种蛋白质，其中血红素活性位点在结构和功能上均完整（UV-vis、圆二色性和共振拉曼），并且在双(4-吡啶基)二硫化物修饰的金电极。
The preparation and spectrophotometric characterization of (both Fe2+ and Fe3+ forms) poly(ethylene glycol) (PEG; av FW 5000)-modified horse cytochrome c (cyt c(PEG)n) with different degrees of modification (n(av) = 6, 19) by UV-vis spectroscopy, circular dichroism spectroscopy, resonance Raman spectroscopy, and cyclic voltammetry are described. Extensive modification (n(av) = 19) of cyt c causes gross structural deformation of the heme as evidenced by major spectral changes in the UV-vis and circular dichroism spectral signatures of both the Fe2+ and Fe3+ forms. Modification of cyt c by six PEG residues, however, produces a protein in which the heme active site is structurally and functionally intact (UV-vis, circular dichroism, and resonance Raman) and which exhibits at least quasireversible direct electron transfer (E-degrees' = 338 +/- 5 mV vs SHE; (2.1 +/- 0.6) x 10(-3) cm/s) at bis(4-pyridyl) disulfide-modified Au electrodes.