Paramagnetic 1H NMR Spectroscopy to Investigate the Catalytic Mechanism of Radical S-Adenosylmethionine Enzymes

被引：20

作者：

Camponeschi, Francesca ^{[1
,2
,3
]}

Muzzioli, Riccardo ^{[1
,2
,3
]}

Ciofi-Baffoni, Simone ^{[1
,2
,3
]}

Piccioli, Mario ^{[1
,2
,3
]}

Banci, Lucia ^{[1
,2
,3
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr CERM, Via Luigi Sacconi 6, I-50019 Florence, Italy

[2] Univ Florence, Dept Chem, Via Lastruccia 3, I-50019 Florence, Italy

[3] Univ Texas MD Anderson Canc Ctr, Dept Canc Syst Imaging, 1881 East Rd,3SCR4-3600,Unit 1907, Houston, TX 77054 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2019年 / 431卷 / 22期

关键词：

Lipoyl synthase; Iron-sulfur proteins; Enzyme mechanism; Electron transfer; Metallo enzyme; IRON-SULFUR PROTEIN; NUCLEAR-MAGNETIC-RESONANCE; COLI LIPOYL SYNTHASE; ESCHERICHIA-COLI; ELECTRONIC-STRUCTURE; CHROMATIUM-VINOSUM; 4FE-4S CLUSTER; INSERTION; FERREDOXINS; SUBSTRATE;

D O I：

10.1016/j.jmb.2019.08.018

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Iron-sulfur clusters in radical S-adenosylmethionine (SAM) enzymes catalyze an astonishing array of complex and chemically challenging reactions across all domains of life. Here we showed that H-1 NMR spectroscopy experiments tailored to reveal hyperfine-shifted signals of metal-ligands is a powerful tool to monitor the binding of SAM and of the octanoyl-peptide substrate to the two [4Fe-4S] clusters of human lipoyl synthase. The paramagnetically shifted signals of the iron-ligands were specifically assigned to each of the two bound [4Fe-4S] clusters, and then used to examine the interaction of SAM and substrate molecules with each of the two [4Fe-4S] clusters of human lipoyl synthase. H-1 NMR spectroscopy can therefore contribute to the description of the catalityc mechanism of radical SAM enzymes. (C) 2019 Elsevier Ltd. All rights reserved.

引用

页码：4514 / 4522

页数：9

共 50 条

[1] Paramagnetic Intermediates Generated by Radical S-Adenosylmethionine (SAM) Enzymes
Stich, Troy A.
Myers, William K.
Britt, R. David
ACCOUNTS OF CHEMICAL RESEARCH, 2014, 47 (08) : 2235 - 2243
[2] S-Adenosylmethionine radical enzymes
Marsh, ENG
Patwardhan, A
Huhta, MS
BIOORGANIC CHEMISTRY, 2004, 32 (05) : 326 - 340
[3] Radical S-Adenosylmethionine Enzymes
Broderick, Joan B.
Duffus, Benjamin R.
Duschene, Kaitlin S.
Shepard, Eric M.
CHEMICAL REVIEWS, 2014, 114 (08) : 4229 - 4317
[4] Radical S-adenosylmethionine enzymes: Mechanism, control and function
Challand, Martin R.
Driesener, Rebecca C.
Roach, Peter L.
NATURAL PRODUCT REPORTS, 2011, 28 (10) : 1696 - 1721
[5] Snapshots of S-adenosylmethionine radical enzymes
Drennan, Catherine
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2015, 250
[6] The Catalytic Mechanism of the Class C Radical S-Adenosylmethionine Methyltransferase NosN
Ding, Wei
Li, Yongzhen
Zhao, Junfeng
Ji, Xinjian
Mo, Tianlu
Qianzhu, Haocheng
Tu, Tao
Deng, Zixin
Yu, Yi
Chen, Fener
Zhang, Qi
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2017, 56 (14) : 3857 - 3861
[7] Complex Biotransformations Catalyzed by Radical S-Adenosylmethionine Enzymes
Zhang, Qi
Liu, Wen
JOURNAL OF BIOLOGICAL CHEMISTRY, 2011, 286 (35) : 30245 - 30252
[8] Radical S-Adenosylmethionine Enzymes in Human Health and Disease
Landgraf, Bradley J.
McCarthy, Erin L.
Booker, Squire J.
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85, 2016, 85 : 485 - 514
[9] Radical S-Adenosylmethionine Enzymes Involved in RiPP Biosynthesis
Mahanta, Nilkamal
Hudson, Graham A.
Mitchell, Douglas A.
BIOCHEMISTRY, 2017, 56 (40) : 5229 - 5244
[10] The structure and catalytic mechanism of the S-adenosylmethionine dependent radical enzyme biotin synthase
Jarrett, J
Wan, J
Dotson, M
Reyda, M
Drennan, C
Berkovitch, F
Nicolet, Y
FASEB JOURNAL, 2004, 18 (08): : C222 - C223

← 1 2 3 4 5 →