Mechanism of the enzymic reduction of N2: the binding of adenosine 5'-triphosphate and cyanide to the N2-reducing system.
Mechanism of the enzymic reduction of N2: the binding of adenosine 5'-triphosphate and cyanide to the N2-reducing system.
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N2 酶促还原机制：5-三磷酸腺苷和氰化物与 N2 还原系统的结合。
DOI：
10.1073/pnas.61.3.1021
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发表时间：
1968
影响因子：
11.1
通讯作者：
L. Mortenson
中科院分区：
文献类型：
--
作者：
P. T. Bui;L. Mortenson
N_2 的体外还原是一个复杂的过程，涉及至少六种不同的反应物：两种蛋白质 [1,2]（已被命名为偶氮铁氧还蛋白 (AzoFd) 和钼铁氧还蛋白 (MoFd)[3]）、电子源、电子受体、ATP[4] 和 Mg2+[5-7]。该领域研究的目标之一是定义这些反应物的有序和定量参与，导致电子受体的还原，同时 ATP 分解为 ADP 和无机磷酸盐[7]。
本文描述的工作表明（1）AzoFd 可逆地结合 ATP（N2 还原中的反应物）和 ADP（N2 还原的特异性抑制剂）；（2）MoFd 可逆地结合氰化物，氰化物也被 N_2 还原系统还原。推测ATP与氰化物的结合是N_2还原系统的部分反应。
The in vitro reduction of N_2 is a complex process involving at least six different reactants: two proteins [1,2] for which the names azoferredoxin (AzoFd) and molybdoferredoxin (MoFd) have been proposed[3], an electron source, the electron acceptor, ATP[4], and Mg2+[5-7]. One of the goals of research in this area is to define the orderly and quantitative participation of these reactants leading to the reduction of the electron acceptor with concomitant breakdown of ATP to ADP and inorganic phosphate[7].
The work described in this paper shows that (1) AzoFd reversibly binds both ATP, a reactant in N2 reduction, and ADP, a specific inhibitor of N2 reduction, and (2) MoFd reversibly binds cyanide, which is also reduced by the N_2-reducing system. It is suggested that the binding of ATP and of cyanide are partial reactions of the N_2-reducing system.