X-ray analysis of ferredoxin from Spirulina platensis. II. Chelate structure of active center.
X-ray analysis of ferredoxin from Spirulina platensis. II. Chelate structure of active center.
复制标题
钝顶螺旋藻铁氧还蛋白的 X 射线分析。
DOI：
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发表时间：
1978
期刊：
影响因子：
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通讯作者：
H. Matsubara
中科院分区：
文献类型：
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作者：
T. Tsukihara;K. Fukuyama;H. Tahara;Y. Katsube;Y. Matsuura;N. Tanaka;M. Kakudo;K. Wada;H. Matsubara
A chloroplast-type ferredoxin from Spirulina platenis crystallized in an orthorhombic system, space group C2221, with cell dimensions a=62.32, b=28.51, and c=108.08 A. The electron density map at 2.8 A resolution was prepared by using the best phase angles determined by the single isomorphous replacement method coupled with the anomalous dispersion method. The chelating structure of the acitve center was revealed as follows. Of the six cysteinyl residues in the molecule, Cys 41, Cys 4k, Cys 49, and Cys 79 are involved in the active center. Cys 41 and Cys 46 are coordinated to one iron atom, and Cys 49 and Cys 79 to the other iron atom. Only one of these cysteinyl residues, Cys 79, is comparatively apart from the other three in the amino acids sequence of the molecule, as found in the case of bacterial ferredoxin. It appears that the NH....S hydrogen bonds are around the active center, as in other non-heme iron sulfur proteins.
