Tedro S M, Meyer T E, Kamen M D
J Biol Chem. 1979 Mar 10;254(5):1495-500.
The amino acid sequence of a high oxidation-reduction potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium Rhodospirillum tenue has been determined. This is the smallest of the HiPIP's, containing 63 residues, with only 3 residues apparently conserved in addition to the 4 cluster-binding cysteines. A minimum of four internal genetic gaps is postulated to align tenue high potential iron-sulfur protein with the previously known proteins. It is the most divergent of its class, with an average of only 25% identically matching residues in common with any of the other species.
已确定从紫色光合细菌细螺旋体中分离出的高氧化还原电位铁硫蛋白（HiPIP）的氨基酸序列。这是最小的HiPIP，含有63个残基，除了4个与簇结合的半胱氨酸外，只有3个残基明显保守。推测至少有四个内部遗传缺口才能使细螺旋体高电位铁硫蛋白与先前已知的蛋白质对齐。它是其类别中差异最大的，与任何其他物种的平均相同匹配残基仅为25%。
