Biological pincer complexes.

Biological pincer complexes.
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DOI:
10.1002/cctc.202000575
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发表时间:
2020-09-04
期刊:
影响因子:
4.5
通讯作者:
Hausinger RP
Hausinger RP
中科院分区:
化学3区
文献类型:
--
作者:
Nevarez J;Turmo A;Hu J;Hausinger RP

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已知生物学中至少存在两种类型的钳形复合体。金属吡咯喹啉醌(PQQ)辅因子首先在细菌甲醇脱氢酶中被发现,后来也在其他微生物的短链醇脱氢酶中被发现。根据酶序列,PQQ相关金属可以是钙、镁或稀土元素。这种有机配体的合成需要一系列辅助蛋白质作用于小肽PqqA。金属与PQQ的结合产生ONO型钳形络合物。最近,在乳酸消旋酶LarA中发现了镍钳核苷酸(NPN)辅因子。这种辅因子通过羧化酶/水解酶、硫转移酶和镍插入酶的作用衍生自烟酸腺嘌呤二核苷酸,产生SCS型钳形复合物。NPN辅因子可能存在于细菌、古细菌和少数真核生物的选定的其他消旋酶和差向异构酶中。金属钳形络合物的生物学代表包括在选定的酶中与钙、镁或镧系金属结合的吡咯并喹啉醌(M-PQQ)和某些消旋酶和差向异构酶的镍钳形核苷酸(Ni-NPN)辅因子。
At least two types of pincer complexes are known to exist in biology. A metal-pyrroloquinolone quinone (PQQ) cofactor was first identified in bacterial methanol dehydrogenase, and later also found in selected short-chain alcohol dehydrogenases of other microorganisms. The PQQ-associated metal can be calcium, magnesium, or a rare earth element depending on the enzyme sequence. Synthesis of this organic ligand requires a series of accessory proteins acting on a small peptide, PqqA. Binding of metal to PQQ yields an ONO-type pincer complex. More recently, a nickel-pincer nucleotide (NPN) cofactor was discovered in lactate racemase, LarA. This cofactor derives from nicotinic acid adenine dinucleotide via action of a carboxylase/hydrolase, sulfur transferase, and nickel insertase, resulting in an SCS-type pincer complex. The NPN cofactor likely occurs in selected other racemases and epimerases of bacteria, archaea, and a few eukaryotes. Biological representatives of metal-pincer complexes include pyrroloquinoline quinone bound to calcium, magnesium, or lanthanide metals (M-PQQ) in selected dehydrogenases and nickel-pincer nucleotide (Ni-NPN) cofactors of certain racemases and epimerases.
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