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685 results on '"Penner-Hahn, James E."'

161. Zinc catalyzed alkyl-transfer enzymes

Author

Penner-Hahn, James E., primary, Tobin, Daniel, additional, Matthews, Rowena G., additional, Fierke, Carol A., additional, Peariso, Katrina, additional, Grahame, David A., additional, and Garrow, Timothy A., additional

Published
2003
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167. Corrections

Author

Zhou, Zhaohui S., Peariso, Katrina, Penner-Hahn, James E., and Matthews, Rowena G.

Subjects
Enzymes -- Structure-activity relationship, Ligand binding (Biochemistry) -- Analysis, Biological sciences, Chemistry
Published
2001

173. Electrochemical and Structural Investigation of the Mechanism of Irreversibility in Li3V2(PO4)3Cathodes

Author

Kim, Soojeong, Zhang, Zhengxi, Wang, Senlin, Yang, Li, Cairns, Elton J., Penner-Hahn, James E., and Deb, Aniruddha

Abstract

Lithium-ion batteries dominate the battery field, particularly for electric and hybrid vehicles. Monoclinic Li3V2(PO4)3has emerged as one of the most promising candidates for the cathode in lithium-ion batteries, offering better environmental safety and lower cost than competing materials. We have used in situX-ray absorption spectroscopy to characterize the evolution of the vanadium in a Li3V2(PO4)3cathode as it is cycled electrochemically. These data demonstrate the presence of significant kinetic effects such that the measured electrochemical behavior does not represent the bulk vanadium. When the cell is cycled between 3 and 4.5 V, there are two distinct vanadium species. When the potential is raised above 4.5 V, a third species is observed, consistent with formation of V5+. XANES data for the cathode after 3–4.8 V cycling are consistent with a severely distorted vanadium site, suggesting that lithium–vanadium antisite mixing may be responsible for the electrochemical irreversibility that is seen above 4.5 V.

Published
2016
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181. A De Novo Designed Metalloenzyme for the Hydration of CO2.

Author

Cangelosi, Virginia M., Deb, Aniruddha, Penner-Hahn, James E., and Pecoraro, Vincent L.

Subjects
METALLOENZYMES, HYDRATION, HYDRATASES, CATALYSIS, AFFINITY labeling
Abstract

Protein design will ultimately allow for the creation of artificial enzymes with novel functions and unprecedented stability. To test our current mastery of nature's approach to catalysis, a ZnII metalloenzyme was prepared using de novo design. α3DH3 folds into a stable single-stranded three-helix bundle and binds ZnII with high affinity using His3O coordination. The resulting metalloenzyme catalyzes the hydration of CO2 better than any small molecule model of carbonic anhydrase and with an efficiency within 1400-fold of the fastest carbonic anhydrase isoform, CAII, and 11-fold of CAIII. [ABSTRACT FROM AUTHOR]

Published
2014
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182. A De Novo Designed Metalloenzyme for the Hydration of CO2.

Author

Cangelosi, Virginia M., Deb, Aniruddha, Penner-Hahn, James E., and Pecoraro, Vincent L.

Subjects
CARBON dioxide, PROTEIN engineering, SYNTHETIC enzymes, HYDRATION, CARBONIC anhydrase, METALLOENZYMES
Abstract

Protein design will ultimately allow for the creation of artificial enzymes with novel functions and unprecedented stability. To test our current mastery of nature’s approach to catalysis, a ZnII metalloenzyme was prepared using de novo design. α3DH3 folds into a stable single‐stranded three‐helix bundle and binds ZnII with high affinity using His3O coordination. The resulting metalloenzyme catalyzes the hydration of CO2 better than any small molecule model of carbonic anhydrase and with an efficiency within 1400‐fold of the fastest carbonic anhydrase isoform, CAII, and 11‐fold of CAIII. [ABSTRACT FROM AUTHOR]

Published
2014
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184. NMR characterization of substrate binding in the phthalate dioxygenase system

Author

Tierney, David L., Gassner, George T., Luchinat, Claudio, Bertini, Ivavno, Ballou, David P., and Penner-Hahn, James E.

Subjects
Bacterial proteins -- Research, Ligand binding (Biochemistry) -- Research, Metal ions -- Research, Phthalates -- Research, Biological sciences, Chemistry
Abstract

Research was conducted to determine the position of the phthalate with respect to the mononuclear metal ion in native and metal-substituted derivatives of phthalate dioxygenase (PDO) using the paramagnetic enhancements in the NMR relaxation rates for the fluorine in fluorophthalates. Results reveal that the substrate interacts with the mononuclear metal of PDO and, thus, provide the first structural characterization of the interaction.

Published
1999

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