STUDIES ON THE CHEMICAL NATURE OF CLOSTRIDIAL FERREDOXIN.
STUDIES ON THE CHEMICAL NATURE OF CLOSTRIDIAL FERREDOXIN.
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梭菌铁氧化还原蛋白化学性质的研究。
DOI：
10.1016/s0021-9258(18)51805-6
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发表时间：
1963
期刊：
影响因子：
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通讯作者：
J. Rabinowitz
中科院分区：
文献类型：
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作者：
W. Lovenberg;B. Buchanan;J. Rabinowitz
铁氧还蛋白是一种非血红素含铁蛋白，由Mortenson、Valentine和Carnahan从巴氏梭菌中分离得到（2-4）。这种蛋白质对于丙酮酸经二乙氨基乙基纤维素处理的提取物形成乙酰磷酸和氢是必需的，并且显然是连接丙酮酸脱氢酶和氢化酶的电子传递因子。铁氧还蛋白随后在许多厌氧生物中发现，但在需氧或兼性生物中未发现（4，5）。在所有六种梭菌中检测到（5），在甲烷杆菌（5）、消化链霉菌（4）和乳酸微球菌（6，7）中检测到，并且从嗜热厌氧菌热解糖梭菌中分离出一种异常热稳定的铁氧还蛋白（8）。据报道，铁氧还蛋白参与多种反应。它是M还原有机酸、无机化合物和辅酶的必需条件。lactilyticus（7）; C.巴氏杆菌（9-11）;以及酸尿梭菌（12）的二磷酸吡啶核苷酸。也有报道说，它刺激甲烷产生的提取物中的M。omelianskii（13）.在这些酶联反应中对铁氧还蛋白的需要通常通过在添加的或内源性氢化酶存在下将反应与氢利用偶联来证明。巴氏杆菌铁氧还蛋白可以取代先前由San Pietro和Lang（15）从菠菜中分离出的以及由Hill和Bendall（16）从欧芹中结晶出的光合吡啶核苷酸还原酶。据信，它在植物中作为光活化叶绿素分子的初始电子受体发挥作用，并且是TPN光还原（17）和磷酸化（18）所必需的。
Ferredoxin, a nonheme iron-containing protein, was isolated from Clostridium pasteurianum by Mortenson, Valentine, and Carnahan (2-4). This protein is essential for the formation of acetyl phosphate and hydrogen from pyruvate by diethylaminoethyl cellulose-treated extracts of that organism, and is apparently the electron transport factor linking pyruvate dehydrogenase and hydrogenase. Ferredoxin has subsequently been found in many anaerobic but not in aerobic or facultative organisms (4, 5). It has been detected in all of six clostridial species examined (5) and in Methanobacillus omelianskii (5), Peptostreptococcus elsdenii (4), and Micrococcus lactilyticus (6, 7)) and an unusually heat-stable ferredoxin was isolated from the thermophilic anaerobe, Clostridium thermosaccharolyticum (8). Ferredoxin has been reported to be involved in a wide variety of reactions. It is required for the reduction of organic acids, inorganic compounds, and coeneymes by M. lactilyticus (7); of triphosphopyridine nucleotide, hydroxylamine, and nitrite by C. pasteurianum (9-11); and of diphosphopyridine nucleotide by Clostridium acidi-urici(12). It has also been reported to stimulate methane production in extracts of M. omelianskii (13). The requirement for ferredoxin in these ensymic reactions has usually been demonstrated by coupling the reaction with hydrogen utilization in the presence of added or endogenous hydrogenase.Tagawa and Arnon (14) demonstrated that C. pasteurianum ferredoxin can replace the photosynthetic pyridine nucleotide reductase previously isolated from spinach by San Pietro and Lang (15) and crystallized from parsley by Hill and Bendall (16). It is believed to function in plants as the initial electron acceptor of the photoactivated chlorophyll molecule and is required for the photoreduction of TPN (17) and for photophosphorylation (18).