Volume 65, Issue 3 p. 286-293
Original Article

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

Scott Huston

Department of Chemistry, Rutgers University‐Camden, Camden, NJ, USA

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John Collins

Department of Chemistry, Rutgers University‐Camden, Camden, NJ, USA

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Fangfang Sun

Cell Free Bioinnovations Inc., Blacksburg, VA, USA

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Ting Zhang

Department of Chemistry, Rutgers University‐Camden, Camden, NJ, USA

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Timothy D. Vaden

Department of Chemistry and Biochemistry, Rowan University, Glassboro, NJ, USA

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Y.‐H. Percival Zhang

Cell Free Bioinnovations Inc., Blacksburg, VA, USA

Department of Biological Systems Engineering, Virginia Tech, VA, USA

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Jinglin Fu

Corresponding Author

Department of Chemistry, Rutgers University‐Camden, Camden, NJ, USA

Center for Computational and Integrative Biology, Rutgers University‐Camden, Camden, NJ, USA

Address for correspondence: Jinglin Fu, Department of Chemistry, Rutgers University‐Camden, 315 Penn Street, NJ 08102, USA. e‐mail: jinglin.fu@rutgers.edu.Search for more papers by this author
First published: 07 September 2017
Citations: 1

Scott Huston and John Collins have contributed equally to this work.

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.