Iron–sulfur cluster with double duty

IF 44.6 1区 化学 Q1 CHEMISTRY, PHYSICAL
Olga A. Esakova, Squire J. Booker
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引用次数: 0

Abstract

The radical S-adenosylmethionine (SAM) enzyme, AbmM, catalyses a replacement of the ring oxygen of a sugar with sulfur. However, how this reaction takes place is unknown. Now, an [Fe4S4] cluster is shown to have a dual role in catalysis. It functions in the reductive cleavage of SAM and is the donor of the appended sulfur atom.

Abstract Image

Abstract Image

具有双重作用的铁硫簇
自由基s -腺苷甲硫氨酸(SAM)酶,AbmM,催化糖的环氧被硫取代。然而,这种反应是如何发生的尚不清楚。现在,一个[Fe4S4]簇被证明在催化中具有双重作用。它在SAM的还原裂解中起作用,并且是附加的硫原子的供体。
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来源期刊
Nature Catalysis
Nature Catalysis Chemical Engineering-Bioengineering
CiteScore
52.10
自引率
1.10%
发文量
140
期刊介绍: Nature Catalysis serves as a platform for researchers across chemistry and related fields, focusing on homogeneous catalysis, heterogeneous catalysis, and biocatalysts, encompassing both fundamental and applied studies. With a particular emphasis on advancing sustainable industries and processes, the journal provides comprehensive coverage of catalysis research, appealing to scientists, engineers, and researchers in academia and industry. Maintaining the high standards of the Nature brand, Nature Catalysis boasts a dedicated team of professional editors, rigorous peer-review processes, and swift publication times, ensuring editorial independence and quality. The journal publishes work spanning heterogeneous catalysis, homogeneous catalysis, and biocatalysis, covering areas such as catalytic synthesis, mechanisms, characterization, computational studies, nanoparticle catalysis, electrocatalysis, photocatalysis, environmental catalysis, asymmetric catalysis, and various forms of organocatalysis.
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