"Light Regulation Of Flavin Reduction By NAD(P)H: Activation Of 2-haloa" by Karina Kizjakina, Yumin Dai et al.
 

Light Regulation Of Flavin Reduction By NAD(P)H: Activation Of 2-haloacrylate Hydratase

Abstract

We report a novel light-dependent activation mechanism for 2-haloacrylate hydratase (2HAH), a flavin-dependent dehalogenase. Initial assays revealed inconsistent enzyme activity, stabilized only after chemical reduction or exposure to bright light. Spectroscopic analysis showed that light accelerates flavin reduction by NAD(P)H, completing in 30 s under bright light versus slow reduction in the dark. Blue light specifically triggered full activation, while red light had no effect. Sequence and structural analyses indicate that 2HAH does not share homology with known light-sensitive flavoproteins, suggesting an uncharacterized regulatory mechanism. These findings advance our understanding of flavin enzyme regulation and introduce light as a potential tool for modulating 2HAH activity.

Department(s)

Arts, Languages, and Philosophy

Comments

National Science Foundation, Grant CHE 2003658

Keywords and Phrases

Covalent adduct; Dehalogenation reactions; Flavoenzyme; Light activation

International Standard Serial Number (ISSN)

1096-0384; 0003-9861

Document Type

Article - Journal

Document Version

Citation

File Type

text

Language(s)

English

Rights

© 2025 Elsevier, All rights reserved.

Publication Date

01 Feb 2025

PubMed ID

39746390

Link to Full Text

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