Di-iron-carboxylate proteins
Di-iron-carboxylate proteins
复制标题
DOI：
10.1016/0959-440x(95)80008-5
复制
发表时间：
1995-12-01
影响因子：
6.8
通讯作者：
Eklund, H
中科院分区：
文献类型：
--
作者：
Nordlund, P;Eklund, H
由羧酸残基和氧化物/氢氧化物基团桥接的二铁中心到目前为止已经在涉及双氧化学或磷酰基转移反应的四类蛋白质中看到。这些蛋白质中的双核铁中心由组氨酸和额外的羧酸配体协调。这些酶的最新结构数据，结合光谱和动力学数据，现在可以作为详细的机制建议的基础。在主要类别的羟化酶-氧化酶，其中包含核糖核苷酸还原酶和甲烷单加氧酶的二铁网站，显示出显着的灵活性，在其协调的几何形状的三个或更多的羧酸基团。这种灵活性，结合相对较低的配位数和适合活性氧化学的埋藏环境，解释了它们对分子氧氧化能力的有效利用。
Di-iron centers bridged by carboxylate residues and oxide/hydroxide groups have so far been seen in four classes of proteins involved in dioxygen chemistry or phosphoryl transfer reactions. The dinuclear iron centers in these proteins are coordinated by histidines and additional carboxylate ligands. Recent structural data on some of these enzymes, combined With spectroscopic and kinetic data, can now serve as a base for detailed mechanistic suggestions. The di-iron sites in the major class of hydroxylase-oxidase enzymes, which contains ribonucleotide reductase and methane monooxygenase, show significant flexibility in the geometry of their coordination of three or more carboxylate groups. This flexibility, combined with a relatively low coordination number, and a buried environment suitable for reactive oxygen chemistry, explains their efficient harnessing of the oxidation power of molecular oxygen.