Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding

Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding

Abstract Escherichia coli NADPH-dependent assimilatory sulfite reductase (SiR) reduces sulfite by six electrons to make sulfide for incorporation into sulfur-containing biomolecules. SiR has two subunits: an NADPH, FMN, and FAD-binding diflavin flavoprotein and a siroheme/Fe4S4 cluster-containing he...

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Main Authors: Behrouz Ghazi Esfahani, Nidhi Walia, Kasahun Neselu, Yashika Garg, Mahira Aragon, Isabel Askenasy, Hui Alex Wei, Joshua H. Mendez, M. Elizabeth Stroupe
Format: Article
Language:English
Published: Nature Portfolio 2025-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-58037-5
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https://doi.org/10.1038/s41467-025-58037-5

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