Harker A R, Zuber M, Evans H J
J Bacteriol. 1986 Feb;165(2):579-84. doi: 10.1128/jb.165.2.579-584.1986.
Two polypeptides present in aerobic and anaerobic cultures of Escherichia coli HB101 were shown to cross-react with antibodies to the 30- and 60-kilodalton (kDa) subunits of the uptake hydrogenase of Rhizobium japonicum. The cross-reactive polypeptides in a series of different E. coli strains are of Mrs ca. 60,000 and 30,000, and both polypeptides are present in proportion to measurable hydrogen uptake (Hup) activity (r = 0.95). The 60-kDa polypeptide from E. coli HB101 comigrated on native gels with detectable Hup activity. The exact role of the 30-kDa polypeptide in E. coli is unclear. E. coli MBM7061, a natural Hup- variant, grown anaerobically or aerobically lacked detectable Hup activity and failed to cross-react with the antisera against the hydrogenase from R. japonicum. Anaerobically cultured E. coli MBM7061, however, did express formate hydrogenlyase activity, indicating that the hydrogenases involved in the oxygen-dependent activation of hydrogen and the formate-dependent evolution of hydrogen are biochemically distinct.
研究表明，大肠杆菌HB101需氧和厌氧培养物中的两种多肽与针对日本根瘤菌摄取氢化酶30千道尔顿（kDa）和60千道尔顿亚基的抗体发生交叉反应。一系列不同大肠杆菌菌株中的交叉反应性多肽分子量约为60,000和30,000，且这两种多肽的存在比例与可测量的氢气摄取（Hup）活性相关（r = 0.95）。大肠杆菌HB101的60-kDa多肽在天然凝胶上与可检测到的Hup活性共迁移。30-kDa多肽在大肠杆菌中的具体作用尚不清楚。大肠杆菌MBM7061是一种天然的Hup变体，无论厌氧还是需氧培养均缺乏可检测到的Hup活性，且不能与抗日本根瘤菌氢化酶的抗血清发生交叉反应。然而，厌氧培养的大肠杆菌MBM7061确实表达甲酸氢化酶活性，这表明参与氧气依赖型氢气活化和甲酸依赖型氢气释放的氢化酶在生化性质上是不同的。
