An activity transition from NADH dehydrogenase to NADH oxidase during protein denaturation

May 22, 2018

Title

An activity transition from NADH dehydrogenase to NADH oxidase during protein denaturation

Author

Scott Huston, John Collins, Fangfang Sun, Ting Zhang, Timothy D. Vaden, Y.-H. Percival Zhang, Jinglin Fu

Year

2017

Journal

Biotechnology and Applied Biochemistry

Abstract

A decrease in the specific activity of an enzyme is commonly observed when the enzyme is inappropriately handled or is stored over an extended period. Here, we reported a functional transition of an FMN-bound diaphorase (FMN–DI) that happened during the long-term storage process. It was found that FMN–DI did not simply lose its β-nicotinamide adenine diphosphate (NADH) dehydrogenase activity after a long-time storage, but obtained a new enzyme activity of NADH oxidase. Further mechanistic studies suggested that the alteration of the binding strength of an FMN cofactor with a DI protein could be responsible for this functional switch of the enzyme.

Instrument

J-810

Keywords

Circular dichroism, Secondary structure, Protein folding, Soret, Ligand binding, Biochemistry