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首页> 外文期刊>plant and cell physiology >FA/FBProtein from the Spinach Photosystem I Complex: Isolation in a Native State and Some Properties of the Iron-Sulfur Clusters
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FA/FBProtein from the Spinach Photosystem I Complex: Isolation in a Native State and Some Properties of the Iron-Sulfur Clusters

机译:来自菠菜光系统 I 复合物的 FA/FBProtein:天然状态下的分离和铁硫团簇的一些特性

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The FA/FBprotein of the photosystem I complex was isolated from spinach leaves in a native state by use of anaerobic systems. The protein contained 8.5 non-heme iron atoms and 8.0 acid-labile sulfur atoms per molecule, consistent with the current concept that it has two 4Fe-4S clusters. Its absorption spectrum was very similar to those of bacterial-type ferredoxins. The ratio of the absorbance at 390 nm to that at 280 nm was 0.6, and the molar extinction coefficient at 390 nm was 32,000 M−.cm−.The oxidation-reduction properties of the iron-sulfur clusters were examined by redox potentiometry and EPR spectroscopy. The two clusters were distinguishable in terms of their oxidation-reduction midpoint potentials; their Emvalues were determined to be about-470 mV and-560 mV, respectiv
机译:利用厌氧系统从天然状态的菠菜叶中分离出光系统I复合物的FA/FB蛋白。该蛋白质每个分子含有 8.5 个非血红素铁原子和 8.0 个酸不稳定硫原子,与目前它有两个 [4Fe-4S] 簇的概念一致。其吸收谱与细菌型铁氧还蛋白的吸收谱非常相似。采用氧化还原电位法和EPR光谱法研究了铁硫团簇在390 nm处的吸光度比值为0.6,摩尔消光系数为32,000 M−.cm−。这两个团簇在氧化还原中点电位方面是可区分的;它们的赋值被确定为约-470 mV和-560 mV,尊重

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