Cosper Michele Mader, Jameson Guy N L, Davydov Roman, Eidsness Marly K, Hoffman Brian M, Huynh Boi Hanh, Johnson Michael K
Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602, USA.
J Am Chem Soc. 2002 Nov 27;124(47):14006-7. doi: 10.1021/ja0283044.
The combination of resonance Raman, electron paramagnetic resonance and Mössbauer spectroscopies has been used to investigate the effect of S-adenosyl-l-methionine (SAM) on the spectroscopic properties of the [4Fe-4S]2+ cluster in biotin synthase. The results indicate that SAM interacts directly at a unique iron site of the [4Fe-4S]2+ cluster in BioB and support the hypothesis of a common inner-sphere mechanism for the reductive cleavage of SAM in the radical SAM family of Fe-S enzymes.
共振拉曼光谱、电子顺磁共振光谱和穆斯堡尔光谱相结合，已被用于研究S-腺苷-L-甲硫氨酸（SAM）对生物素合酶中[4Fe-4S]2+簇光谱性质的影响。结果表明，SAM在BioB中[4Fe-4S]2+簇的一个独特铁位点上直接相互作用，并支持了铁硫酶自由基SAM家族中SAM还原裂解的常见内球机制假说。
