Duschene Kaitlin S, Veneziano Susan E, Silver Sunshine C, Broderick Joan B
Department of Chemistry and Biochemistry, Montana State University, Bozeman, 59717, United States.
Curr Opin Chem Biol. 2009 Feb;13(1):74-83. doi: 10.1016/j.cbpa.2009.01.022. Epub 2009 Mar 9.
The radical AdoMet superfamily comprises a diverse set of >2800 enzymes that utilize iron-sulfur clusters and S-adenosylmethionine (SAM or AdoMet) to initiate a diverse set of radical-mediated reactions. The intricate control these enzymes exercise over the radical transformations they catalyze is an amazing feat of elegance and sophistication in biochemistry. This review focuses on the accumulating evidence for how these enzymes control this remarkable chemistry, including controlling the reactivity between the iron-sulfur cluster and AdoMet, and controlling the subsequent radical transformations.
自由基腺苷甲硫氨酸超家族包含2800多种不同的酶，这些酶利用铁硫簇和S-腺苷甲硫氨酸（SAM或AdoMet）引发一系列不同的自由基介导反应。这些酶对其催化的自由基转化进行的精细控制是生物化学中一项令人惊叹的优雅而复杂的壮举。本综述重点关注这些酶如何控制这种非凡化学反应的越来越多的证据，包括控制铁硫簇与腺苷甲硫氨酸之间的反应性，以及控制随后的自由基转化。
