초록
<P>Our research demonstrated that novel pentamethylcyclopentadienyl (Cp*) iridium pyridine sulfonamide complex PySO<SUB>2</SUB>NPh-Ir (<B>7</B>) could highly specifically catalyze nicotinamide adenine dinucleotide (NAD<SUP>+</SUP>) into the corresponding reducing cofactor NADH in cell growth media containing various biomolecules. The structures and catalytic mechanism of <B>7</B> were studied by single-crystal X-ray, NMR, electrochemical, and kinetic methods, and the formation of iridium hydride species Ir-H was confirmed to be the plausible hydride-transfer intermediate of <B>7</B>. Moreover, benefiting from its high hydrogen-transfer activity and selectivity for NADH regeneration, <B>7</B> was used as an optimal metal catalyst to establish a chem-enzyme cascade catalytic hydrogen-transfer system, which realized the high-efficiency preparation of <SMALL>L</SMALL>-glutamic acid by combining with <SMALL>L</SMALL>-glutamate dehydrogenase (GLDH).</P><P>This research demonstrated that novel pentamethylcyclopentadienyl (Cp*) iridium pyridine sulfonamide complex PySO<SUB>2</SUB>NPh-Ir (<B>7</B>) could highly effectively and specifically catalyze the reduction of nicotinamide adenine dinucleotide (NAD<SUP>+</SUP>) into the corresponding reducing cofactor NADH in cell growth media using HCOONa as a hydrogen source. Moreover, <B>7</B> was used as an optimal metal catalyst to establish a chem-enzyme cascade catalytic hydrogen-transfer system, which realized the high-efficiency preparation of <SMALL>L</SMALL>-glutamic acid by combining with <SMALL>L</SMALL>-glutamate dehydrogenase (GLDH).</P><BR>[FIG OMISSION]</BR>