Measurement and ab initio calculation of CSA/dipole- dipole cross-correlated relaxation provide insight into the mechanism of a H2-forming dehydrogenase

被引：7

作者：

Bartoschek, S

Buurman, G

Geierstanger, BH

Lapham, J

Griesinger, C

机构：

[1] Univ Marburg, Max Planck Inst Terr Mikrobiol, D-35043 Marburg, Germany

[2] Univ Marburg, Mikrobiol Lab, Fachbereich Biol, D-35043 Marburg, Germany

[3] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany

[4] Genom Inst Novartis Res Fdn, San Diego, CA 92121 USA

[5] Fed Univ Rio De Janeiro, Ctr Nacl Ressonancia Magnet Nucl, BR-21941590 Rio De Janeiro, Brazil

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2003年 / 125卷 / 44期

关键词：

2-DIMENSIONAL NMR-SPECTROSCOPY; METAL-FREE HYDROGENASE; TENSORIAL INTERACTIONS; THYMIDYLATE SYNTHASE; METHANOGENIC ARCHAEA; ANGLES; STEREOSPECIFICITY; SUBSTRATE;

D O I：

10.1021/ja029953i

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Using transferred cross-correlated relaxation and DFT calculations, the conformation of the relevant conformation of N5,N10-methylenetetrahydromethanopterin, a reaction intermediate bound to the 80 kD H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase is determined. The conformation of the intermediate differs from the free form in solution and makes the reaction mechanism plausible. Copyright © 2003 American Chemical Society.

引用

页码：13308 / 13309

页数：2

共 19 条

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Bartoschek S, 2001, CHEMBIOCHEM, V2, P530, DOI 10.1002/1439-7633(20010803)2:7/8<530::AID-CBIC530>3.3.CO

[2]

2-S

[3] Transferred cross-correlated relaxation complements transferred NOE: Structure of an IL-4R-derived peptide bound to STAT-6 [J].