文章基本信息

标题：The Isolation and Characterization of a New Iron-Sulfur Protein from Photosynthetic Membranes
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作者：Richard Malkin ; Pedro J. Aparicio ; Daniel I. Arnon 等
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：6
页码：2362-2366
DOI：10.1073/pnas.71.6.2362
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：A new iron-sulfur protein, distinct from the soluble chloroplast ferredoxin, was isolated from chloroplast membranes. The isolated protein, purified to homogeneity, had a molecular weight of about 8000 and 4 atoms of iron and 4 inorganic sulfides per mole. Its absorption spectrum had a broad absorbance band in the 400 nm region, a shoulder at approximately 310 nm, and a peak around 280 nm. The absorbance ratio A400 to A280 was 0.55. The electron paramagnetic resonance spectrum (measured at 12{degrees}K) of the reduced protein was similar to that of other reduced iron-sulfur proteins, showing a major resonance line at g = 1.94. The isolated protein, when photoreduced by spinach chloroplasts, can in turn transfer electrons to mammalian cytochrome c. However, the photoreduced protein cannot replace soluble ferredoxin in NADP+ reduction because of its apparent inability to interact with the chloroplast enzyme, ferredoxin-NADP+ reductase. The relation of the isolated iron-sulfur protein to the bound ferredoxin that acts as the primary electron acceptor in Photosystem I is discussed.
关键词：photosynthesis ; chloroplasts ; ferredoxins ; electron carriers