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首页> 外文期刊>Chinese science bulletin >Retrospect and prospect of some proposed 'string-bag' structure models for the active center of nitrogenase
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Retrospect and prospect of some proposed 'string-bag' structure models for the active center of nitrogenase

机译：提出的一些针对固氮酶活性中心的“线袋”结构模型的回顾与展望

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The problem of how the nitrogenase is capable of transforming dinitrogen into ammonia has indeed become one of the hot subjects in the field of molecular biochemistry. In 1992, Kim and Rees of the California Institute of Technology published their result of the crystal structure analysis carried out for the Av nitrogenase with a resolution of 0.27 nm. After that, in cooperation with Chan, they have been able to carry out the crystal analysis with a further resolution of 0.22nm, and proposed structuremodels for the active center of the FeMo cofactor and the P-cluster pair. Meanwhile, Bolin and Morgan as well as their groups of the Purdue University and the University of Georgia have also published their result of the Cp nitrogenase with the resolution refined to 0.22 run. These new important crystallographic results feature a big step forward in the structural work on nitrogenase. The structure model for the active center of the FeMo cofactor proposed by both the Rees group and the Bolin group resemble each other very well in the fact that it is made up of two 'string-bags' Mo(Fe_3S_3) and Fe(Fe_3S_3) coupled 'neck-to-neck' with a quasi-mirror S-'Y'-S plane in between, resulting in an approximate C_(3h) point group symmetry. The only difference between the two structure models is the triad of coupling atoms, namely two S atoms and one 'Y' atom (either O or N) for the Rees structure, whereas it is a triad of S atoms for the Bolin structure. Thus each 'string-bag' has the structure of a puckered Fe_3S_3 6-membered ring capped by a transition-metal atom M (Mp or Fe); and the coupling 'waist' is a tricyclic cluster of three condensed puckered Fe_4S_4 8-membered octagonal rings (see figure 1(a), (b)).
机译：固氮酶如何能够将二氮转化为氨的问题确实已经成为分子生物化学领域中的热门话题之一。 1992年，加利福尼亚理工学院的Kim和Rees发表了他们对Av固氮酶进行的晶体结构分析的结果，其分辨率为0.27 nm。之后，他们与Chan合作，能够以0.22nm的进一步分辨率进行晶体分析，并提出了FeMo辅因子和P簇对的活性中心的结构模型。同时，Bolin和Morgan以及普渡大学和乔治亚大学的研究小组也发布了Cp固氮酶的结果，其分辨率提高到0.22 run。这些新的重要晶体学结果表明，在固氮酶结构研究中迈出了一大步。里斯（Rees）组和波林（Bolin）组提出的FeMo辅因子活性中心的结构模型非常相似，因为它由两个“袋” Mo（Fe_3S_3）和Fe（Fe_3S_3）组成。将“颈对颈”与准镜S-'Y'-S平面之间耦合，从而产生近似C_（3h）点组对称性。两种结构模型之间的唯一区别是耦合原子的三单元组，即对于Rees结构，是两个S原子和一个'Y'原子（O或N），而对于Bolin结构，则是S原子的三单元组。因此，每个“线袋”都具有一个折叠的Fe_3S_3 6元环结构，该环被过渡金属原子M（Mp或Fe）覆盖；耦合的“腰部”是三个缩合的折叠的Fe_4S_4 8元八角形环的三环簇（见图1（a），（b））。

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