J
James E. Penner-Hahn
Researcher at University of Michigan
Publications - 238
Citations - 13380
James E. Penner-Hahn is an academic researcher from University of Michigan. The author has contributed to research in topics: Extended X-ray absorption fine structure & Absorption spectroscopy. The author has an hindex of 64, co-authored 233 publications receiving 12592 citations. Previous affiliations of James E. Penner-Hahn include University at Buffalo & Stanford University.
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Journal ArticleDOI
Antivitamins B12 in a Microdrop: The Excited-State Structure of a Precious Sample Using Transient Polarized X-ray Absorption Near-Edge Structure.
Nicholas A. Miller,Lindsay B Michocki,Roberto Alonso-Mori,Alexander Britz,Aniruddha Deb,Daniel P. DePonte,James M. Glownia,April K Kaneshiro,Christoph Kieninger,Jake Koralek,Joseph H Meadows,Tim Brandt van Driel,Bernhard Kräutler,Kevin J. Kubarych,James E. Penner-Hahn,Roseanne J. Sension +15 more
TL;DR: Polarized transient X-ray absorption near-edge structure (XANES) was used to probe the excited-state structure of a photostable B12 antivitamin, suggesting that the acetylide linkage raises the barrier for expansion of the Co-C bond.
Journal ArticleDOI
NSLS X-19A beamline performance for X-ray absorption measurements
TL;DR: The X-19 beamline at the National Synchrotron Light Source (NSLS) as discussed by the authors was designed for high-resolution X-ray absorption spectroscopy over a wide energy range.
Journal ArticleDOI
Snapshots of transition states
TL;DR: Time-resolved X-ray absorption has been used to investigate the structure of the Zn active site in alcohol dehydrogenase during catalysis and supports a new mechanistic model for catalysis.
Journal ArticleDOI
Structural characterization of the zinc site in Escherichia coliL-threonine dehydrogenase using extended X-ray absorption fine structure spectroscopy
TL;DR: The EXAFS data reported here and the thiol/disulfide levels determined for TDH, together with the homology of TDH to horse liver alcohol dehydrogenase, suggest that the one Zn2+/subunit ofTDH is non-catalytic and is probably bound by cysteine residues 93, 96, 99, and 107 in a structural zinc-binding loop of the protein.
Journal ArticleDOI
Structural Characterization of Horseradish Peroxidase Using EXAFS Spectroscopy. Evidence for Fe=O Ligation in Compounds I and II
James E. Penner-Hahn,K S Eble,Thomas J. McMurry,Mark W. Renner,Alan L. Balch,Jay T. Groves,John H. Dawson,Keith O. Hodgson +7 more
TL;DR: In this article, the authors used extended X-ray absorption fine structure spectroscopy to determine the structural environment of the heme iron sites in horseradish peroxidase compounds I and II.