Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase - structural models of the short-lived oxygen complexes
Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase - structural models of the short-lived oxygen complexes
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DOI：
10.1016/s0003-9861(02)00555-6
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发表时间：
2003-01-01
影响因子：
3.9
通讯作者：
Schlichting, I
中科院分区：
文献类型：
--
作者：
Fedorov, R;Ghosh, DK;Schlichting, I
测定了P450 cam和樟脑的三元氰化物配合物的晶体结构，其分辨率为1.8埃，并发现与活性氧配合物的结构相同[I. Schlichting等人，2000，Science 287，1615]。值得注意的是，氰化物以弯曲模式结合，并诱导活性构象，其特征在于存在两个水分子和保守的Asp 251的羰基翻转。氰化物、L-精氨酸和诱导型一氧化氮合酶的加氧酶结构域的三元复合物的结构被确定为2.4埃分辨率。氰化物基本上线性结合，与L-Arg相互作用，并诱导活性位点处的水分子结合。这种水通过主链相互作用定位，位于距氰化物的氮原子2.8埃处，并且可以提供一氧化氮合酶的羟基化反应中O-O键断裂所需的质子。(C)2002 Elsevier Science（美国）。All rights reserved.
The crystal structure of the ternary cyanide complex of P450cam and camphor was determined to 1.8 Angstrom resolution and found to be identical with the structure of the active oxygen complex [I. Schlichting et al., 2000, Science 287, 1615]. Notably, cyanide binds in a bent mode and induces the active conformation that is characterized by the presence of two water molecules and a flip of the carbonyl of the conserved Asp251. The structure of the ternary complex of cyanide, L-arginine, and the oxygenase domain of inducible nitric oxide synthase was determined to 2.4 Angstrom resolution. Cyanide binds essentially linearly, interacts with L-Arg, and induces the binding of a water molecule at the active site. This water is positioned by backbone interactions, located 2.8 Angstrom from the nitrogen atom of cyanide, and could provide a proton required for O-O bond scission in the hydroxylation reaction of nitric oxide synthase. (C) 2002 Elsevier Science (USA). All rights reserved.