通过脉冲辐解在水溶液中形成超还原型嗜铬菌属高电位铁硫蛋白。
Formation of super-reduced Chromatium high-potential iron--sulphur protein in aqueous solution by pulse radiolysis.
作者信息
Butler J, Sykes A G, Buxton G V, Harrington P C, Wilkins R G
出版信息
Biochem J. 1980 Sep 1;189(3):641-4. doi: 10.1042/bj1890641.
Abstract
Both the oxidized and reduced forms of Hipip (high-potential iron--sulphur protein) are reduced (approx. 30% yields) by eaq.- in a single-stage process, rate constants 1.7 x 10(10) and 1.8 x 10(10) M-1 . s-1 respectively, at 25 degrees C, pH 7.0 (5 mM-phosphate). Super-reduced Hipip, which is formed in the latter case, has a spectrum which closely resembles that of reduced ferredoxin, i.e. Fe4S4 (SR)4(3-) clusters. The spectrum is stable over 2 s periods investigated. Super-reduced Hipip is reoxidized with O2, rate constant 4.8 x 10(6) M-1 . s-1 at 25 degrees C.
摘要
高电位铁硫蛋白（Hipip）的氧化态和还原态在单步过程中均被水合电子还原（产率约为30%），在25℃、pH 7.0（5 mM磷酸盐）条件下，速率常数分别为1.7×10¹⁰和1.8×10¹⁰ M⁻¹·s⁻¹。在后一种情况下形成的超还原态Hipip具有与还原型铁氧化还原蛋白相似的光谱，即Fe₄S₄(SR)₄³⁻簇。在所研究的2 s时间段内，该光谱是稳定的。超还原态Hipip会被O₂再氧化，在25℃时速率常数为4.8×10⁶ M⁻¹·s⁻¹。
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本文引用的文献
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Molar extinction coefficient and iron and sulfide content of clostridial ferredoxin.梭菌铁氧化还原蛋白的摩尔消光系数以及铁和硫化物含量
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The complete amino acid sequence of Chromatium high potential iron sulfur protein.嗜色菌高电位铁硫蛋白的完整氨基酸序列。
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"Super-reduction" of chromatium high-potential iron-sulphur protein in the presence of dimethyl sulphoxide.在二甲基亚砜存在下铬高电位铁硫蛋白的“超还原”
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