期刊
JOURNAL OF CHEMICAL PHYSICS
卷 135, 期 5, 页码 -出版社
AMER INST PHYSICS
DOI: 10.1063/1.3623418
关键词
enzymes; hydrogen bonds; infrared spectra; molecular biophysics; molecular configurations
资金
- NIH [R01 GM79368, R01 GM65368]
- NSF [CHE-0644410, CHE-0715448]
- BSF [2007256]
Mid-IR active analogs of enzyme cofactors have the potential to be important spectroscopic reporters of enzyme active site dynamics. Azido-nicotinamide adenine dinucleotide (NAD(+)), which has been recently synthesized in our laboratory, is a mid-IR active analog of NAD(+), a ubiquitous redox cofactor in biology. In this study, we measure the frequency-frequency time correlation function for the antisymmetric stretching vibration of the azido group of azido-NAD(+) in water. Our results are consistent with previous studies of pseudohalides in water. We conclude that azido-NAD(+) is sensitive to local environmental fluctuations, which, in water, are dominated by hydrogen-bond dynamics of the water molecules around the probe. Our results demonstrate the potential of azido-NAD(+) as a vibrational probe and illustrate the potential of substituted NAD(+)-analogs as reporters of local structural dynamics that could be used for studies of protein dynamics in NAD-dependent enzymes. (C) 2011 American Institute of Physics. [doi:10.1063/1.3623418]
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