Departments of Microbiology & Molecular Genetics and Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
Curr Opin Struct Biol. 2019 Dec;59:1-8. doi: 10.1016/j.sbi.2018.12.008. Epub 2019 Feb 1.
A vast array of metal cofactors are associated with the active sites of metalloenzymes. This Opinion describes the most recently discovered metal cofactor, a nickel-pincer nucleotide (NPN) coenzyme that is covalently tethered to lactate racemase from Lactobacillus plantarum. The enzymatic function of the NPN cofactor and its pathway for biosynthesis are reviewed. Furthermore, insights are summarized from recent advances involving other selected organometallic and inorganic-cluster cofactors including the lanthanide-pyrroloquinoline quinone found in certain alcohol dehydrogenases, tungsten-pyranopterins or molybdenum-pyranopterins in chosen enzymes, the iron-guanylylpyridinol cofactor of [Fe] hydrogenase, the nickel-tetrapyrrole coenzyme F430 of methyl coenzyme M reductase, the vanadium-iron cofactor of nitrogenase, redox-dependent rearrangements of the nickel-iron-sulfur C-cluster in carbon monoxide dehydrogenase, and light-dependent changes in the multi-manganese cluster of the oxygen-evolving complex.
大量的金属辅因子与金属酶的活性位点有关。本观点描述了最近发现的一种镍钳核苷酸（NPN）辅酶，它与植物乳杆菌的乳酸消旋酶共价连接。综述了 NPN 辅因子的酶学功能及其生物合成途径。此外，还总结了最近在其他选定的有机金属和无机簇辅酶方面的进展，包括某些醇脱氢酶中的镧系吡咯并喹啉醌、某些酶中的钨吡喃并蝶呤或钼吡喃并蝶呤、[Fe]氢化酶中的铁鸟苷基吡啶醇辅因子、甲基辅酶 M 还原酶的镍四吡咯辅酶 F430、固氮酶的钒铁辅因子、一氧化碳脱氢酶中镍铁硫 C 簇的氧化还原依赖性重排以及产氧复合物中多锰簇的光依赖性变化。
