ArticleThe journal of physical chemistry. B2012
3-picolyl azide adenine dinucleotide as a probe of femtosecond to picosecond enzyme dynamics.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Semiartificial COChemical reviews · 2026Review
- Anisotropic dynamics of an interfacial enzyme active site observed using tethered substrate analogs and ultrafast 2D IR spectroscopy.The Journal of chemical physics · 2023Article
- Transparent window 2D IR spectroscopy of proteins.The Journal of chemical physics · 2021Review
- Extending the vibrational lifetime of azides with heavy atoms.Physical chemistry chemical physics : PCCP · 2020Article
- Heterogeneous and Highly Dynamic Interface in Plastocyanin-Cytochrome f Complex Revealed by Site-Specific 2D-IR Spectroscopy.The journal of physical chemistry. B · 2019Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Article
- Applications of two-dimensional infrared spectroscopy.The Analyst · 2015Review
- Line shape analysis of two-dimensional infrared spectra.The Journal of chemical physics · 2015Article
- Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015Review
- General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins.The journal of physical chemistry. B · 2014Article
- An alternative structural isoform in amyloid-like aggregates formed from thermally denatured human γD-crystallin.Protein science : a publication of the Protein Society · 2014Article
- Sensitive, site-specific, and stable vibrational probe of local protein environments: 4-azidomethyl-L-phenylalanine.The journal of physical chemistry. B · 2013Article
- A strongly absorbing class of non-natural labels for probing protein electrostatics and solvation with FTIR and 2D IR spectroscopies.The journal of physical chemistry. B · 2013Article
- Hydrogen tunneling links protein dynamics to enzyme catalysis.Annual review of biochemistry · 2013Review
- Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Topics in current chemistry · 2013Review
Corrections and comments
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Authors and funding
6 authors.
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Abstract
Functionally relevant femtosecond to picosecond dynamics in enzyme active sites can be difficult to measure because of a lack of spectroscopic probes that can be located in the active site without altering the behavior of the enzyme. We have developed a new NAD(+) analog 3-Picolyl Azide Adenine Dinucleotide (PAAD(+)), which has the potential to be a general spectroscopic probe for NAD-dependent enzymes. This analog is stable and binds in the active site of a typical NAD-dependent enzyme formate dehydrogenase (FDH) with characteristics similar to those of natural NAD(+). It has an isolated infrared transition with high molar absorptivity that makes it suitable for observing enzyme dynamics using 2D IR spectroscopy. 2D IR experiments show that in aqueous solution, the analog undergoes complete spectral diffusion within hundreds of femtoseconds consistent with the water hydrogen bonding dynamics that would be expected. When bound to FDH in a binary complex, it shows picosecond fluctuations and a large static offset, consistent with previous studies of the binary complexes of this enzyme. These results show that PAAD(+) is an excellent probe of local dynamics and that it should be a general tool for probing the dynamics of a wide range of NAD-dependent enzymes.
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