Mammalian Flavoproteome Analysis Using Label-Free Quantitative Mass Spectrometry

Abstract

Human flavin cofactor-containing enzymes constitute a small, but highly important flavoproteome. Its stability is required to ensure key metabolic functions, such as oxidative phosphorylation and beta-oxidation of fatty acid. Flavoproteome disfunction due to mutations of individual proteins or because of the lack of FMN and FAD precursor riboflavin (vitamin B2) results in clinically relevant abnormal cellular states and diseases. Current technical possibilities in the field of the quantitative mass spectrometry of proteins allow studying the flavoproteome changes under different stress conditions, including the deficiency of vitamin B2. The biological readouts of flavoenzyme destabilization, such as protein degradation and aggregation, provide important insights into the molecular mechanisms of metabolic adaptation to nutrient deficiency. The proteomic-scale studies of protein stability have significant novelty potential in basic and applied biomedical research.

Keywords: Flavoproteome; Mass spectrometry; Protein aggregation; Protein degradation; Riboflavin.