ArticleAnalytical biochemistry2010
Characterization of azido-NAD+ to assess its potential as a two-dimensional infrared probe of enzyme dynamics.
Article in Analytical biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Topics in current chemistry · 2013Review
- Synthesis of radiolabeled nicotinamide cofactors from labeled pyridines: versatile probes for enzyme kinetics.Analytical biochemistry · 2012Article
- 3-picolyl azide adenine dinucleotide as a probe of femtosecond to picosecond enzyme dynamics.The journal of physical chemistry. B · 2012Article
- Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.The journal of physical chemistry. B · 2011Article
- Site-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules.The journal of physical chemistry letters · 2011Article
- Two-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water.The Journal of chemical physics · 2011Article
- A direct comparison of azide and nitrile vibrational probes.Physical chemistry chemical physics : PCCP · 2011Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Enzyme active-site dynamics at femtosecond to picosecond time scales are of great biochemical importance, but remain relatively unexplored due to the lack of appropriate analytical methods. Two-dimensional infrared (2D IR) spectroscopy is one of the few methods that can examine chemical biological motions at this time scale, but all the IR probes used so far were specific to a few unique enzymes. The lack of IR probes of broader specificity is a major limitation to further 2D IR studies of enzyme dynamics. Here we describe the synthesis of a general IR probe for nicotinamide-dependent enzymes. This azido analog of the ubiquitous cofactor nicotinamide adenine dinucleotide is found to be stable and bind to several dehydrogenases with dissociation constants similar to that for the native cofactor. The infrared absorption spectra of this probe bound to several enzymes indicate that it has significant potential as a 2D IR probe to investigate femtosecond dynamics of nicotinamide-dependent enzymes.
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