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Here, we investigated lysine acetylation of the 2Fe\u20132S ferredoxin\n                  <jats:italic>Hv<\/jats:italic>\n                  Fdx (HVO_2995) and its flavin-dependent oxidoreductase\n                  <jats:italic>Hv<\/jats:italic>\n                  FdR (HVO_2345) partner in the halophilic archaeon\n                  <jats:italic>Haloferax volcanii<\/jats:italic>\n                  . Genetic and biochemical analyses established\n                  <jats:italic>Hv<\/jats:italic>\n                  Fdx as an essential 2Fe\u20132S ferredoxin with a midpoint redox potential of \u2212385 mV. Lysine acetylation of\n                  <jats:italic>Hv<\/jats:italic>\n                  Fdx was found to occur primarily at K119, a residue positioned near the [Fe-S] cluster interface, and to modulate electron transfer capacity without impacting Fe\u2013S cluster incorporation, midpoint potential, or protein abundance. In contrast,\n                  <jats:italic>Hv<\/jats:italic>\n                  FdR was found lysine acetylated at multiple sites in a manner consistent with a non-enzymatic mechanism that resulted in altered flavin binding, enzymatic activity, and thermal stability. Lysine acetylation of\n                  <jats:italic>Hv<\/jats:italic>\n                  Fdx was found to stimulate electron flow from\n                  <jats:italic>Hv<\/jats:italic>\n                  FdR as measured by an anaerobic NADPH \u2192\n                  <jats:italic>Hv<\/jats:italic>\n                  FdR \u2192\n                  <jats:italic>Hv<\/jats:italic>\n                  Fdx \u2192 DCIP assay. 3D structural modeling, proteomic, biochemical, and genetic assays suggest the haloarchaeal GNAT-family acetyltransferase homolog HVO_2874 as a candidate enzyme associated with\n                  <jats:italic>Hv<\/jats:italic>\n                  Fdx lysine acetylation and optimal growth of\n                  <jats:italic>H. volcanii<\/jats:italic>\n                  . Together, these findings demonstrate that lysine acetylation differentially regulates archaeal redox-active proteins and functions as an important mechanism coordinating redox metabolism in\n                  <jats:italic>H. volcanii<\/jats:italic>\n                  .\n                <\/jats:p>","DOI":"10.64898\/2026.08.10.743930","type":"posted-content","created":{"date-parts":[[2026,8,11]],"date-time":"2026-08-11T04:25:15Z","timestamp":1786422315000},"source":"Crossref","is-referenced-by-count":0,"title":["Lysine acetylation-mediated regulation of ferredoxin and ferredoxin reductase redox-active proteins in\n                  <i>Haloferax volcanii<\/i>"],"prefix":"10.64898","author":[{"given":"Katherine R.","family":"Weber","sequence":"first","affiliation":[{"name":"Department of Microbiology and Cell Science, Institute of Food and Agricultural Science, University of Florida, Gainesville, FL, 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