1.12.1.2 4Fe-4S-center presence of a 4Fe-4S-center in addition to the active site iron 724910 1.12.1.2 ATP 30% stimulation 439699 1.12.1.2 benzyl viologen oxidized and reduced 439633, 656298 1.12.1.2 Ferredoxin the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically for catalysis of H2 production 712281 1.12.1.2 flavin 1 molecule of FMN per enzyme molecule 439703 1.12.1.2 flavin 2 molecules of FMN per enzyme molecule 439710 1.12.1.2 flavin flavoprotein 439699, 439703, 439710 1.12.1.2 flavin only when FMN or riboflavin are added in combination with Mg2+ or Ni2+, NAD-reducing system is activated 439701 1.12.1.2 FMN - 712281 1.12.1.2 FMN 1 FMN molecule per enzyme molecule 439703 1.12.1.2 FMN 2 FMN molecules per enzyme molecule 439710 1.12.1.2 FMN 2 molecules per enzyme molecule, one of 2 can be reversibly released upon reduction of the enzyme 656298 1.12.1.2 FMN 25% stimulation 439699 1.12.1.2 FMN bound to the diaphorase subunits 654782 1.12.1.2 FMN cofactor and stabilization of the active site 724910 1.12.1.2 FMN enzyme contains FMN 744926 1.12.1.2 FMN module HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters 726282 1.12.1.2 FMN required, 2 molecules per tetrameric enzyme complex, reduced enzyme reversibly releases half of the FMN bound, kinetics, FMN release induces reduction with NADH, overview 656298 1.12.1.2 FMN required, enzyme contains 1 mol FMN per mol of enzyme 656734 1.12.1.2 iron-sulfur centre - 687407, 689959 1.12.1.2 additional information benzyl viologen, methyl viologen or methylene blue can replace NAD+/NADH 654388 1.12.1.2 additional information methyl viologen can replace NAD+/NADH 655638 1.12.1.2 additional information methyl viologen or benzyl viologen can replace NAD+/NADH 656734 1.12.1.2 additional information methyl viologen or dithionite can act as electron donor/acceptor 654821 1.12.1.2 additional information methyl viologen, oxidized and reduced can replace NAD+/NADH 655307 1.12.1.2 additional information Ni-Fe cofactor, analysis of the non-standard structure of the Ni-Fe cofactor bound at the active site, interaction mechanism with H2, structural changes during reaction, reduction, and inactivation, the cofactor structure is (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO), overview 654562 1.12.1.2 additional information no activity with ferredoxin or FMN 654821 1.12.1.2 additional information no activity with NADP+ 655890 1.12.1.2 additional information no activity with NADPH and NADP+ 654388 1.12.1.2 additional information no activity with NADPH/NADP+ 656734 1.12.1.2 NAD(P)+ - 654821 1.12.1.2 NAD(P)H NADH is 2times more active than NADPH 654821 1.12.1.2 NAD+ - 439633, 654285, 654562, 655307, 655638, 655890, 656298, 685324 1.12.1.2 NAD+ dependent on 654388 1.12.1.2 NAD+ dependent on, binding site on the diaphorase subunits 654782 1.12.1.2 NAD+ highly specific for 656734 1.12.1.2 NADH - 439633, 654285, 654562, 655307, 655638, 656298, 704606, 712972 1.12.1.2 NADH dependent on 654388 1.12.1.2 NADH dependent on, binding site on the diaphorase subunits 654782 1.12.1.2 NADH highly specific for 656734 1.12.1.2 NADH the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically for catalysis of H2 production 712281 1.12.1.2 NADPH - 704606 1.12.1.2 [2Fe-2S]-center HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters 726282 1.12.1.2 [4Fe-4S]-center HoxFU accommodates a [2Fe2S] cluster, FMN and a series of [4Fe4S] clusters 726282