Tedro S M, Meyer T E, Kamen M D
Arch Biochem Biophys. 1985 Sep;241(2):656-64. doi: 10.1016/0003-9861(85)90592-2.
The amino acid sequences of high-redox-potential ferredoxin (HiPIP) isozymes from Ectothiorhodospira halophila have been determined. These are: isozyme I, EPRAEDGHAHDYVNEAADPSHGRYQEGQLCENCAFWGEAVQDGWGRCTHPDFDEVLVKAEGWCSVYAPA S, and isozyme II, GLPDGVEDLPKAEDDHAHDYVNDAADTDHARFQEGQLCENCQFWVDYVNGWGYCQHPDFTDVLVRGEGW CSVYAPA. Isozyme II is the major form of HiPIP produced by the bacterium (65-80%) and is the most acidic of the known HiPIPs. The two isozymes are 72% identical to one another and require only a single residue deletion for alignment. Comparison of these HiPIPs with seven previously determined sequences revealed only 27% average identity. Both E. halophila HiPIP isozymes are likely to be functional since their sequences are equally distant from those of other species. The E. halophila HiPIP sequences show that H-bonding patterns recognized in Chromatium vinosum HiPIP are likely to be conserved and therefore cannot explain the unusually low redox potentials which have been reported.
已测定了嗜盐外硫红螺菌中高氧化还原电位铁氧化还原蛋白（HiPIP）同工酶的氨基酸序列。这些序列如下：同工酶I，EPRAEDGHAHDYVNEAADPSHGRYQEGQLCENCAFWGEAVQDGWGRCTHPDFDEVLVKAEGWCSVYAPA S；同工酶II，GLPDGVEDLPKAEDDHAHDYVNDAADTDHARFQEGQLCENCQFWVDYVNGWGYCQHPDFTDVLVRGEGW CSVYAPA。同工酶II是该细菌产生的HiPIP的主要形式（65 - 80%），并且是已知HiPIP中酸性最强的。这两种同工酶彼此间有72%的同一性，对齐时仅需一个残基缺失。将这些HiPIP与之前测定的七个序列进行比较，发现平均同一性仅为27%。嗜盐外硫红螺菌的两种HiPIP同工酶可能都具有功能，因为它们的序列与其他物种的序列距离相等。嗜盐外硫红螺菌的HiPIP序列表明，在嗜硫葡糖杆菌HiPIP中识别出的氢键模式可能是保守的，因此无法解释所报道的异常低的氧化还原电位。
