| Literature DB >> 24634364 |
Zac Long1, Jeff Maltas, Michael C Zatt, Jun Cheng, Erik J Alquist, Alex Brest, Paul Urayama.
Abstract
The cellular proportion of free and protein-bound NADH complexes is increasingly recognized as a metabolic indicator and biomarker. Because free and bound forms exhibit different fluorescence spectra, we consider whether autofluorescence shape sufficiently correlates with mitochondrial metabolism to be useful for monitoring in cellular suspensions. Several computational approaches for rapidly quantifying spectrum shape are used to detect Saccharomyces cereviseae response to oxygenation, and to the addition of mitochondrial functional modifiers and metabolic substrates. Observed changes appear consistent with previous studies probing free/protein-bound proportions, making this a potentially useful approach for the real-time monitoring of metabolism. (Entities:
Keywords: NADH; autofluorescence; fluorescence spectroscopy; mitochondrial metabolism
Mesh:
Substances:
Year: 2014 PMID: 24634364 DOI: 10.1002/jbio.201300207
Source DB: PubMed Journal: J Biophotonics ISSN: 1864-063X Impact factor: 3.207