期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 142, 期 3, 页码 1457-1464出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b11506
关键词
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资金
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [SPP 1927, LE 2934/1-1]
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy [EXC 2008/1 - 390540038]
- Einstein Center of Catalysis (EC2)
[NiFe] hydrogenases catalyze the reversible oxidation of molecular hydrogen into two protons and two electrons. A key organometallic chemistry feature of the NiFe active site is that the iron atom is co-coordinated by two cyanides (CN-) and one carbon monoxide (CO) ligand. Biosynthesis of the NiFe(CN)(2)(CO) cofactor requires the activity of at least six maturation proteins, designated HypA-F. An additional maturase, HypX, is required for CO ligand synthesis under aerobic conditions, and preliminary in vivo data indicated that HypX releases CO using N-10-formyltetrahydrofolate (N-10-formyl-THF) as the substrate. HypX has a bipartite structure composed of an N-terminal module similar to N-10-formyl-THF transferases and a C-terminal module homologous to enoyl-CoA hydratases/isomerases. This composition suggested that CO production takes place in two consecutive reactions. Here, we present in vitro evidence that purified HypX first transfers the formyl group of N-10-formyl-THF to produce formyl-coenzyme A (formyl-CoA) as a central reaction intermediate. In a second step, formyl-CoA is decarbonylated, resulting in free CoA and carbon monoxide. Purified HypX proved to be metal-free, which makes it a unique catalyst among the group of CO-releasing enzymes.
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