Solid state NMR: new tools for insight into enzyme function

被引:47
作者
McDermott, Ann [1 ]
Polenova, Tatyana
机构
[1] Columbia Univ, Dept Chem, New York, NY 10027 USA
[2] Univ Delaware, Dept Chem & Biochem, Newark, DE 19716 USA
基金
美国国家科学基金会;
关键词
D O I
10.1016/j.sbi.2007.10.001
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
NMR has had considerable impact in enzymology, probing evidence for ionization states, conformational 'strain', compressed interactions, electronically unusual species, and conformational dynamics of enzymes. Solid-state NMR is becoming increasingly important in studying enzymes because of a number of recent tools for analysis of proteins by SSNMR, and because of the growing ability to isolate the species of interest for analysis. Here, we review recent studies of a Michaelis complex, of the dynamic functioning of membrane-associated enzymes, and initial studies of several enzymes with redox-active and paramagnetic centers.
引用
收藏
页码:617 / 622
页数:6
相关论文
共 67 条
[1]   Quantifying energetic contributions to ground state destabilization [J].
Anderson, VE .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2005, 433 (01) :27-33
[2]   Internal enzyme motions as a source of catalytic activity: Rate-promoting vibrations and hydrogen tunneling [J].
Antoniou, D ;
Schwartz, SD .
JOURNAL OF PHYSICAL CHEMISTRY B, 2001, 105 (23) :5553-5558
[3]   Effect of enzyme dynamics on catalytic activity [J].
Antoniou, Dinhtri ;
Basner, Jodi ;
Nunez, Sara ;
Schwartz, Steven D. .
ADVANCES IN PHYSICAL ORGANIC CHEMISTRY, VOL 41, 2006, 41 :315-362
[4]   Solid-state NMR of matrix metalloproteinase 12:: An approach complementary to solution NMR [J].
Balayssac, Stephane ;
Bertini, Ivano ;
Faelber, Katja ;
Fragai, Marco ;
Jehle, Stefan ;
Lelli, Moreno ;
Luchinat, Claudio ;
Oschkinat, Hartmut ;
Yeo, Kwon Joo .
CHEMBIOCHEM, 2007, 8 (05) :486-489
[5]   Paramagnetic ions provide structural restraints in solid-state NMR of proteins [J].
Balayssac, Stephane ;
Bertini, Ivano ;
Lelli, Moreno ;
Luchinat, Claudio ;
Maletta, Massimiliano .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2007, 129 (08) :2218-+
[6]   Molecular interactions investigated by multi-dimensional solid-state NMR [J].
Baldus, Marc .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2006, 16 (05) :618-623
[7]   Water-protein hydrogen exchange in the micro-crystalline protein Crh as observed by solid state NMR spectroscopy [J].
Böckmann, A ;
Juy, M ;
Bettler, E ;
Emsley, L ;
Galinier, A ;
Penin, F ;
Lesage, A .
JOURNAL OF BIOMOLECULAR NMR, 2005, 32 (03) :195-207
[8]   An NMR perspective on enzyme dynamics [J].
Boehr, David D. ;
Dyson, H. Jane ;
Wright, Peter E. .
CHEMICAL REVIEWS, 2006, 106 (08) :3055-3079
[9]   A view at the millennium: The efficiency of enzymatic catalysis [J].
Bruice, TC .
ACCOUNTS OF CHEMICAL RESEARCH, 2002, 35 (03) :139-148
[10]   Computational approaches: Reaction trajectories, structures, and atomic motions. Enzyme reactions and proficiency [J].
Bruice, Thomas C. .
CHEMICAL REVIEWS, 2006, 106 (08) :3119-3139