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Metalloproteins: Radical SAM catalysis via an organometallic intermediate with an Fe-[5′-C]-deoxyadenosyl bond

発表形態:
原著論文
主要業績:
主要業績
単著・共著:
共著
発表年月:
2016年05月
DOI:
10.1126/science.aaf5327
会議属性:
指定なし
査読:
有り
リンク情報:

日本語フィールド

著者:
Horitani, Masaki; Shisler, Krista; Broderick, William E.; Hutcheson, Rachel U.; Duschene, Kaitlin S.; Marts, Amy R.; Hoffman, Brian M.; Broderick, Joan B.
題名:
Metalloproteins: Radical SAM catalysis via an organometallic intermediate with an Fe-[5′-C]-deoxyadenosyl bond
発表情報:
Science 巻: 352 号: 6287 ページ: 822-825
キーワード:
概要:
Radical S-adenosylmethionine (SAM) enzymes use a [4Fe-4S] cluster to cleave SAM to initiate diverse radical reactions. These reactions are thought to involve the 5′-deoxyadenosyl radical intermediate, which has not yet been detected. We used rapid freeze-quenching to trap a catalytically competent intermediate in the reaction catalyzed by the radical SAM enzyme pyruvate formate-lyase activating enzyme. Characterization of the intermediate by electron paramagnetic resonance and 13C, 57Fe electron nuclear double-resonance spectroscopies reveals that it contains an organometallic center in which the 5′ carbon of a SAM-derived deoxyadenosyl moiety forms a bond with the unique iron site of the [4Fe-4S] cluster. Discovery of this intermediate extends the list of enzymatic bioorganometallic centers to the radical SAM enzymes, the largest enzyme superfamily known, and reveals intriguing parallels to B12 radical enzymes.
抄録:

英語フィールド

Author:
Horitani, Masaki; Shisler, Krista; Broderick, William E.; Hutcheson, Rachel U.; Duschene, Kaitlin S.; Marts, Amy R.; Hoffman, Brian M.; Broderick, Joan B.
Title:
Metalloproteins: Radical SAM catalysis via an organometallic intermediate with an Fe-[5′-C]-deoxyadenosyl bond
Announcement information:
Science Vol: 352 Issue: 6287 Page: 822-825
An abstract:
Radical S-adenosylmethionine (SAM) enzymes use a [4Fe-4S] cluster to cleave SAM to initiate diverse radical reactions. These reactions are thought to involve the 5′-deoxyadenosyl radical intermediate, which has not yet been detected. We used rapid freeze-quenching to trap a catalytically competent intermediate in the reaction catalyzed by the radical SAM enzyme pyruvate formate-lyase activating enzyme. Characterization of the intermediate by electron paramagnetic resonance and 13C, 57Fe electron nuclear double-resonance spectroscopies reveals that it contains an organometallic center in which the 5′ carbon of a SAM-derived deoxyadenosyl moiety forms a bond with the unique iron site of the [4Fe-4S] cluster. Discovery of this intermediate extends the list of enzymatic bioorganometallic centers to the radical SAM enzymes, the largest enzyme superfamily known, and reveals intriguing parallels to B12 radical enzymes.


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