Nucleotide sequence encoding the flavoprotein and iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex
Nucleotide sequence encoding the flavoprotein and iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex
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编码枯草芽孢杆菌 PY79 琥珀酸脱氢酶复合物的黄素蛋白和铁硫蛋白亚基的核苷酸序列
作者：
M. K. Phillips;L. Hederstedt;S. Hasnain;L. Rutberg;J. Guest
测定了枯草芽孢杆菌琥珀酸脱氢酶的2.7-脱氢酶DNA片段的核苷酸序列，该片段含有编码黄素蛋白（Fp，sdhA）和铁硫蛋白（Ip，sdhB）亚基的sdhA和sdhB基因。该序列延伸了先前报道的编码细胞色素b558亚基（sdhC）的序列，并完成了sdh操纵子sdhCAB的序列。Fp和Ip亚基的预测分子量为65，186（585个氨基酸）和28，285（252个氨基酸），与标记的Fp和Ip抗原独立测定的值一致，尽管似乎B。在大肠杆菌中表达sdhA基因后，枯草杆菌Fp没有功能。这两个亚基与E.大肠杆菌的大小、组成和氨基酸序列。序列同源性分析进一步表明，B. subtilis SDH亚基与E.大肠杆菌，但不如相应的大肠杆菌对密切相关。coli亚单位。最高的序列保守的区域被确定为催化显着的黄素腺嘌呤二核苷酸结合位点和半胱氨酸簇的铁硫中心。
The nucleotide sequence of a 2.7-kilobase segment of DNA containing the sdhA and sdhB genes encoding the flavoprotein (Fp, sdhA) and iron-sulfur protein (Ip, sdhB) subunits of the succinate dehydrogenase of Bacillus subtilis was determined. This sequence extends the previously reported sequence encoding the cytochrome b558 subunit (sdhC) and completes the sequence of the sdh operon, sdhCAB. The predicted molecular weights for the Fp and Ip subunits, 65,186 (585 amino acids) and 28,285 (252 amino acids), agreed with the values determined independently for the labeled Fp and Ip antigens, although it appeared that the B. subtilis Fp was not functional after expression of the sdhA gene in Escherichia coli. Both subunits closely resembled the corresponding Fp and Ip subunits of the succinate dehydrogenase (SDH) and fumarate reductase of E. coli in size, composition, and amino acid sequence. The sequence homologies further indicated that the B. subtilis SDH subunits are equally related to the SDH and fumarate reductase subunits of E. coli but are less closely related than are the corresponding pairs of E. coli subunits. The regions of highest sequence conservation were identifiable as the catalytically significant flavin adenine dinucleotide-binding sites and cysteine clusters of the iron-sulfur centers.
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DOI：
10.1073/pnas.78.11.6749
发表时间：
1981-11
影响因子：
11.1
作者：
S. Vik;Y. Hatefi
通讯作者：
S. Vik;Y. Hatefi
大肠杆菌富马酸还原酶中的高电位铁硫中心是一个三铁簇。
DOI：
--
发表时间：
1985
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Morningstar,JE;Johnson,MK;Cecchini,G;Ackrell,BA;Kearney,EB
通讯作者：
Kearney,EB
2.0 A 分辨率下的铁硫簇和固氮菌铁氧化还原蛋白的蛋白质结构。
影响因子：
5.6
作者：
Ghosh,D;O'Donnell,S;FureyJr,W;Robbins,AH;Stout,CD
通讯作者：
Stout,CD
缺乏共价结合黄素的枯草芽孢杆菌突变体琥珀酸脱氢酶：主要缺陷的鉴定以及突变型和野生型酶中铁硫簇的研究。
影响因子：
2.9
作者：
Maguire,JJ;Magnusson,K;Hederstedt,L
通讯作者：
Hederstedt,L
用乙氧基甲酸酐和玫瑰红对牛心琥珀酸脱氢酶进行修饰：底物保护必需组氨酰残基的证据。
影响因子：
3.9
作者：
Hederstedt,L;Hatefi,Y
通讯作者：
Hatefi,Y