NADPH-dependent sulfite reductase minimal dimer
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ABSTRACT:
SUBMITTER: Margaret Elizabeth Stroupe
PROVIDER: EMPIAR-12180 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structure of dimerized assimilatory NADPH-dependent sulfite reductase reveals the minimal interface for diflavin reductase binding.
Ghazi Esfahani Behrouz B Walia Nidhi N Neselu Kasahun K Garg Yashika Y Aragon Mahira M Askenasy Isabel I Wei Hui Alex HA Mendez Joshua H JH Stroupe M Elizabeth ME
bioRxiv : the preprint server for biology 20250118
<i>Escherichia coli</i> 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/Fe<sub>4</sub>S<sub>4</sub> cluster-containing hemoprotein. The molecular interactions that govern subunit binding have been unknown since the discovery of SiR over 50 years ago because SiR is flexible, thus has been intransigent ...[more]
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