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Desulfovibrio Desulfuricans G20 Tetraheme Cytochrome Structure At 1.5 A˚ And Cytochrome Interaction With Metal Complexes, Mrunalini Pattarkine, J J. Tanner, C A. Bottoms, Y H. Lee, Judy D. Wall May 2006

Desulfovibrio Desulfuricans G20 Tetraheme Cytochrome Structure At 1.5 A˚ And Cytochrome Interaction With Metal Complexes, Mrunalini Pattarkine, J J. Tanner, C A. Bottoms, Y H. Lee, Judy D. Wall

Faculty Works

The structure of the type I tetraheme cytochrome c3 from Desulfovibrio desulfuricans G20 was determined to 1.5 A˚ by X-ray crystallography. In addition to the oxidized form, the structure of the molybdate-bound form of the protein was determined from oxidized crystals soaked in sodium molybdate. Only small structural shifts were obtained with metal binding, consistent with the remarkable structural stability of this protein. In vitro experiments with pure cytochrome showed that molybdate could oxidize the reduced cytochrome, although not as rapidly as U(VI) present as uranyl acetate. Alterations in the overall conformation and thermostability of the metal-oxidized protein were investigated …


Homeland Security: Engaging The Frontlines - Symposium Proceedings, George H. Baker, Cheryl J. Elliott Apr 2006

Homeland Security: Engaging The Frontlines - Symposium Proceedings, George H. Baker, Cheryl J. Elliott

George H Baker

The rise of the American homeland security endeavor under the leadership of the new Department of Homeland Security has been heralded by several major national strategy documents. These documents have served to organize efforts at top levels within the government and industry. However, the national strategy guidance is not getting to many organizations and people at the grass-roots level who can make the most difference in preventing attacks, protecting systems, and recovering from catastrophic events, viz. the general citizenry, private infrastructure owners, and local governments. To better understand grass-roots issues and solutions, James Madison University, in cooperation with the Federal …


Biochemical Characterization Of The Major Sorghum Grain Peroxidase, Mamoudou H. Dicko, Harry Gruppen, Riet Hilhorst, Alphons G. J. Voragen, Willen W. H. Van Berkel Apr 2006

Biochemical Characterization Of The Major Sorghum Grain Peroxidase, Mamoudou H. Dicko, Harry Gruppen, Riet Hilhorst, Alphons G. J. Voragen, Willen W. H. Van Berkel

Pr. Mamoudou H. DICKO, PhD

The major cationic peroxidase in sorghum grain (SPC4) , which is ubiquitously present in all sorghum varieties was purified to apparent homogeneity, and found to be a highly basic protein (pI #1;11). MS analysis showed that SPC4 consists of two glycoforms with molecular masses of 34227 and 35629 Da and it contains a type-b heme. Chemical deglycosylation allowed to estimate sugar contents of 3.0% and 6.7% (w ⁄ w) in glycoform I and II, respectively, and a mass of the apoprotein of 33 246 Da. High performance anion exchange chromatography allowed to determine the carbohydrate constituents of the polysaccharide chains. …