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

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

doi:10.1002/bab.1607

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

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

Chemistry

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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.

Original language	English (US)
Pages (from-to)	286-293
Number of pages	8
Journal	Biotechnology and Applied Biochemistry
Volume	65
Issue number	3
DOIs	https://doi.org/10.1002/bab.1607
State	Published - May 1 2018

All Science Journal Classification (ASJC) codes

Biotechnology
Bioengineering
Molecular Medicine
Biomedical Engineering
Applied Microbiology and Biotechnology
Drug Discovery
Process Chemistry and Technology

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title = "An activity transition from NADH dehydrogenase to NADH oxidase during protein denaturation",

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.",

author = "Scott Huston and John Collins and Fangfang Sun and Ting Zhang and Vaden, {Timothy D.} and Zhang, {Y. H.Percival} and Jinglin Fu",

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AU - Huston, Scott

AU - Collins, John

AU - Sun, Fangfang

AU - Zhang, Ting

AU - Vaden, Timothy D.

AU - Zhang, Y. H.Percival

AU - Fu, Jinglin

PY - 2018/5/1

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AB - 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.

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

Abstract

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