Electron spin resonance was used to confirm the structural changes of iron-sulfur clusters in the presence of different nucleophiles
Recently, using the electron spin resonance spectrometer of the steady-state strong magnetic field experiment device of the Strong Magnetic Field Science Center of the Chinese Academy of Sciences, the Liu Wen research group of the Shanghai Institute of Organic Chemistry of the Chinese Academy of Sciences and the Institute of Applied Physics of the Chinese Academy of Sciences cooperated with S-adenosylmethionine. Free radical enzyme (S-adenosylmethionine, SAM) NosL, a similar enzyme NocL, has been studied in detail. Related results were published in the form of research papers in the recent "Biochemistry Newsletter" (J. Biol. Chem. 2011, doi: 10.1074 / jbc.M111.224832).
Fe-S cluster is the oldest cofactor in biochemistry. Such cofactors are ubiquitous in all kinds of organisms and are widely involved in various life processes. In addition to its most important function for electron transfer, iron-sulfur clusters also catalyze many types of chemical conversions by directly binding to substrates. Due to the important role played by iron-sulfur clusters in biochemistry, their research has always been a hotspot.
Zhang Qi, Liu Wen and others have studied the function of a new type of SAM free radical enzyme NosL (Nat. Chem. Biol. 7, 154). This study found that the iron-sulfur clusters of NocL can not only bind to SAM but also non-specifically bind to L-tryptophan. The experiment confirmed that in the absence of a real substrate, the iron-sulfur clusters of SAM free radical enzyme can bind non-specifically with other nucleophiles, and thus exist in a heterogeneous form. This discovery enriches the current understanding of iron-sulfur clusters, and also has guiding significance for the design of molecular probes and inhibitors for iron-sulfur proteins. In addition, the research also revealed the glycine radical intermediate in the catalytic process.
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