AKAGI J M, CAMPBELL L L
J Bacteriol. 1961 Dec;82(6):927-32. doi: 10.1128/jb.82.6.927-932.1961.
Akagi, J. M. (Western Reserve University, Cleveland, Ohio) and L. Leon Campbell. Studies on thermophilic sulfate-reducing bacteria. II. Hydrogenase activity of Clostridium nigrificans. J. Bacteriol. 82:927-932. 1961.-The hydrogenase of Clostridium nigrificans has been found to be associated with the cell-free particulate fraction which can be sedimented at 105,000 x g in 1 hr. The specific activity of this fraction was increased 2 to 3 fold over that of the crude extract. It was not found possible to liberate the enzyme from the particulate fraction by methods of enzymatic digestion, chemical extraction, or physical disruption. The optimum temperature for H(2) utilization using benzyl viologen as an electron acceptor was found to be 55 C, and the optimum pH range was 7 to 8. Employing metal complexing agents it was found that the enzyme required Fe(++) ions for H(2) utilization. In contrast, Fe(++) ions were not required to catalyze the evolution of H(2) from reduced methyl viologen. The role of Fe(++) ions in the hydrogenase activity of this organism is discussed.
赤木,J.M.(俄亥俄州克利夫兰市西储大学)和L.利昂·坎贝尔。嗜热硫酸盐还原菌的研究。II.黑化梭菌的氢化酶活性。《细菌学杂志》82:927 - 932。1961年。——已发现黑化梭菌的氢化酶与无细胞颗粒部分相关,该部分在105,000×g离心1小时后可沉淀。该部分的比活性比粗提物提高了2至3倍。通过酶消化、化学提取或物理破碎等方法均无法从颗粒部分释放出该酶。以苄基紫精作为电子受体时,利用氢气的最适温度为55℃,最适pH范围为7至8。使用金属络合剂发现,该酶利用氢气需要亚铁离子。相比之下,从还原型甲基紫精催化氢气释放则不需要亚铁离子。本文讨论了亚铁离子在该生物体氢化酶活性中的作用。