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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosus peroxidase at 100 K refined to 1.3 angstrom resolution: coordination geometries of the ligands to the haem iron
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Structures of cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosus peroxidase at 100 K refined to 1.3 angstrom resolution: coordination geometries of the ligands to the haem iron

机译：结构的氰化物,一氧化氮和羟胺复合物的Arthromyces ramosus过氧化物酶在100 K精制1.3埃解析:协调的几何图形配体的血红素铁

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摘要

1.3 angstrom resolution crystal structures of the cyanide, nitric oxide and hydroxylamine complexes of Arthromyces ramosus peroxidase (ARP), a class II peroxidase belonging to the plant peroxidase superfamily, have been determined. Anisotropic temperature factors were introduced for all non-H atoms of these complexes using SHELX-97 and stereochemical constraints were applied to the protein, protoporphyrin and sugar moieties, but not to the coordination geometries to the haem iron. These refinements identified multiple conformations for several side chains and revised the side-chain conformations of several residues. Little difference was observed in the structures of the polypeptides, haem and sugar moieties and in the coordinations to two calcium ions in these complexes. Characteristic coordination geometries of each ligand to the haem iron were observed. CN- binds to the haem iron in a tilt mode (Fe center dot center dot center dot C-N = 170 degrees), whereas NO and hydroxylamine bind in bent modes (Fe center dot center dot center dot N-O = 125 degrees and Fe center dot center dot center dot NH2-OH = 111 degrees). CN- is directed toward the distal histidine (His56) and forms a hydrogen bond with the N-epsilon atom, whereas NO and hydroxylamine are directed away from His56. The Fe atoms of ARP-CN and ARP-NO, in which the haem irons are both in low-spin states, are approximately in the pyrrole N plane, whereas the iron in native ARP, which is in a five-coordinated high-spin state, deviates markedly from the plane.
机译：1.3埃分辨率晶体结构氰化物、一氧化氮和羟胺复合物的Arthromyces ramosus过氧化物酶(ARP),一个类二过氧化物酶属于植物过氧化物酶总科,已经确定。介绍了温度因素non-H使用shelx - 97和原子的复合物被应用于立体化学的约束蛋白质、原卟啉和糖半个,但是血红素不协调的几何图形铁。几个侧链构象和修订几个残基的侧链构象。小观察不同结构多肽的血红素和糖和半个在协调两个钙离子在这些复合物。每个配体的血红素铁观察。CN -结合倾斜模式中的血红素铁(Fe中心导中心导中心点碳氮= 170度),而没有和羟胺绑定弯曲模式(Fe中心导中心导中心点N-O = 125度和铁中心导中心导中心圆点NH2-OH = 111度)。向远端组氨酸(His56)和形式氢键与nε原子,而没有远离His56和羟胺是导演。铁原子ARP-CN ARP-NO,的血红素铁都是low-spin州大约在吡咯N平面,而在一个本地ARP,铁five-coordinated高自旋状态,背离从飞机上显著。

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