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Behrouz Ghazi Esfahani on Muck Rack

Behrouz Ghazi Esfahani

As seen in: BioRxiv
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Articles

Dimerization of assimilatory NADPH-dependent sulfite reductase reveals elements for diflavin reductase binding at a minimal interface

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By Behrouz Ghazi Esfahani, Kasahun Neselu, Yashika Garg, Mahira F. Aragon
| BioRxiv
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 hemoprotein.
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Dimerization of assimilatory NADPH-dependent sulfite reductase reveals elements for diflavin reductase binding at a minimal interface

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By Kasahun Neselu, Mahira F. Aragon, Behrouz Ghazi Esfahani, Isabel Askenasy
| BioRxiv
Abstract Escherichia coli NADPH-dependent assimilatory sulfite reductase is responsible for fixing sulfur for incorporation into sulfur-containing biomolecules. The oxidoreductase is composed of two subunits, an NADPH, FMN, and FAD-binding diflavin reductase and an iron siroheme and Fe4S4-containing oxidase. How they interact has been an unknown for over 50 years because the complex is highly flexible, thus has been intransigent for traditional X-ray or cryo-EM structural analysis.
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