Fast Enzyme Dynamics at the Active Site of Formate Dehydrogenase

Jigar N Bandaria; Samrat Dutta; Sarah E Hill; Amnon Kohen; Christopher M Cheatum

doi:10.1021/ja077599o

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Journal article

Fast Enzyme Dynamics at the Active Site of Formate Dehydrogenase

Jigar N Bandaria, Samrat Dutta, Sarah E Hill, Amnon Kohen and Christopher M Cheatum

Journal of the American Chemical Society, Vol.130(1), pp.22-23

01/01/2008

DOI: 10.1021/ja077599o

PMCID: PMC2533850

PMID: 18067303

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https://www.ncbi.nlm.nih.gov/pmc/articles/2533850View

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Abstract

The role of femtosecond-picosecond structural dynamics of proteins in enzyme-catalyzed reactions is a hotly debated topic. We report infrared photon echo measurement of the formate dehydrogenase-NAD+-azide ternary complex. In contrast to earlier studies of protein dynamics, the data show complete spectral diffusion on the femtosecond-picosecond time scale with no static heterogeneity. This result indicates that this transition-state analogue complex completely samples the distribution of structures that determine the distribution of azide vibrational frequencies within a few picoseconds and that there are no slower motions that perturb the H-bond network at the active site. Copyright © 2008 American Chemical Society.

Details

Title: Subtitle: Fast Enzyme Dynamics at the Active Site of Formate Dehydrogenase
Creators: Jigar N Bandaria - Department of Chemistry and Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242
Samrat Dutta - Department of Chemistry and Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242
Sarah E Hill - Department of Chemistry and Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242
Amnon Kohen - Department of Chemistry and Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242
Christopher M Cheatum - Department of Chemistry and Optical Science and Technology Center, University of Iowa, Iowa City, Iowa 52242
Resource Type: Journal article
Publication Details: Journal of the American Chemical Society, Vol.130(1), pp.22-23
DOI: 10.1021/ja077599o
PMID: 18067303
PMCID: PMC2533850
NLM abbreviation: J Am Chem Soc
ISSN: 0002-7863
eISSN: 1520-5126
Language: English
Date published: 01/01/2008
Academic Unit: Liberal Arts and Science Admin; Chemistry
Record Identifier: 9984216610502771

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