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ISMAR PRIZE AWARDED TO GRIFFIN
The International Society of Magnetic Resonance (ISMAR) has announced that it has awarded its triennial 2010 Prize to Professor Robert G. Griffin. ISMAR awards its prize for outstanding achievement in the field of magnetic resonance.Griffin has made outstanding contributions to NMR spectroscopy, in particular, his successful development of high-field dynamic nuclear polarization (DNP) as a practical method for sensitivity enhancement in solid-state NMR with magic-angle spinning. His contributions have included the design and construction of novel instrumentation for DNP and the use of nitroxide biradicals to improve DNP sensitivity. Griffin and co-workers recently demonstrated the ability of DNP to detect and characterize intermediates in the bacteriorhodopsin photocycle, the widely studied prototype of a ubiquitous family of light-driven ion pumps and a model for other members of the versatile family of retinal pigments, including the G-protein coupled recpetors in the visual system.
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High-Resolution Solid-State NMR Structure of a 17.6 kDa Protein
Ivano Bertini, Anusarka Bhaumik, Gal De Pape, Robert G. Griffin, Moreno Lelli, Jzef R. Lewandowski and Claudio Luchinat
J. Am. Chem. Soc., 2010, 132 (3), pp 1032–1040
Recently the Griffin group, in collaboration with I. Bertini and C. Luchinat and their colleagues from the University of Florence, used high field (850 and 900 MHz) magic angle spinning (MAS) dipolar recoupling NMR to determine the structure of the protein matrix metalloproteinase 12 (MMP12) a 17.6 kD protein, 159 amino acid moiety. Crucial to the completion of the structure was the use of the PAR and PAIN-CP MAS experiments for measuring 13C-13C and 13C-15N distances developed in the Griffin lab [J. Chem. Phys. 129, 245101 (2008)]. The structure has a backbone rmsd of 1.0±0.2 Å, and is therefore high resolution. The strategy used for the structure determination may be generalized for nonmetalloproteins and represents a significant development in protein structure determination protocols using MAS NMR.
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An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
Joseph A. Cotruvo, Jr. and JoAnne Stubbe
Biochemistry, published online January 13, 2010
The Stubbe group has discovered a catalytically active dimanganese(III)-tyrosyl cofactor in the class Ib ribonucleotide reductase (RNR) from Escherichia coli. The class Ib RNRs are the primary aerobic route to the deoxynucleotide building blocks of DNA for many pathogenic bacteria such as Mycobacterium tuberculosis and Bacillus anthracis.
Active cofactor formation requires the presence of a flavodoxin-like protein, NrdI, which we propose reacts with O2 to ultimately form the two equivalents of HO2- required to oxidize a dimanganese(II) cluster to the active dimanganese(III) cluster and tyrosyl radical. We suggest that this newly identified cofactor is likely to be the active form of many class Ib RNRs. Its unique structure and method of biosynthesis offer new targets for antibacterial therapeutics. |
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