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. 2020 Feb 28;11:165. doi: 10.3389/fmicb.2020.00165

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Copyright © 2020 Gao.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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A proposed model for the assembly of Fe–S clusters by SUF system in cyanobacteria. Fe–S cluster biogenesis is initiated by SufS (cysteine desulfurase), which converts cysteine (Cys) to alanine (Ala). Sulfane (S⁰) is transferred from SufS to SufE (sulfur transferase) and then to SufB of SufBC₂D scaffold complex and bound as a persulfide (S^2–). Putative Fe and electron (for reduction S⁰ to S^2–) donors are still unknown. SufC has an ATPase activity, thus coupling ATP hydrolysis with the formation of Fe–S clusters. Subsequently, the newly assembled Fe–S cluster is transferred to the carrier protein, which delivers the Fe–S cluster to apo-protein (Apo) and further converts Apo to holo-protein (Holo). SufA and Slr0067 (Synechocystis 6803) may function as the carrier proteins.