The competition between chemistry and biology in assembling iron–sulfur derivatives. Molecular structures and electrochemistry. Part III. {[Fe2S2](Cys)3(X)} (X=Asp, Arg, His) and {[Fe2S2](Cys)2(His)2} proteins

Nonheme binuclear transition metal complexes with hydrosulfide and polychalcogenides

“…52,53 However, the closely related transition metal-sulfido species are found in the active sites of various important enzymes, which include nitrogenases, [54][55][56][57][58][59][60][61] A cluster and C cluster of [NiFe]-carbon monoxide dehydrogenase (CODH), [62][63][64][65] [MoCu]-CODH, [65][66][67][68] bifunctional CODH/acetyl Co-A Synthase (ACS), 69,70 [Fe-Fe]-hydrogenase, [71][72][73][74] [NiFe]-hydrogenase, 71,74 sulfite reductase [75][76][77][78][79] and aconitase, [80][81][82] as well as that of the electron transfer proteins such as ferredoxins. [83][84][85][86][87][88][89][90] Considering the versatile roles of H 2 S/HS À and S 2À in various biological processes, and the presence of metal-sulfido species in the active sites of various important enzymes, it may be considered that research directed toward the synthesis and reactivity of transition metal complexes featuring HS À and S 2À may help in the understanding and development of bioinorganic chemistry. Consequently, an appreciable number of reports describing the synthesis and characterization...…”

The Redox Active [2Fe-2S] Clusters: Key-Components of a Plethora of Enzymatic Reactions—Part I: Archaea

“…Since we have already dealt with structure and electrochemistry of metalloproteins hosting "classical" ([Fe 2 S 2 ](S γ Cys ) 4 ) and Rieske-type [Fe 2 S 2 ](Cys) 2 (His) 2 ferredoxins [23] as well as "non-classical" [Fe 2 S 2 ](Cys) 3 (X) (X = Asp, Arg, His) [24] ferredoxins, we did not consider them herein.…”

“…In general, Fe-S clusters act as redox-active cofactors of specific enzymatic reacti carried out by many proteins [11][12][13][14][15][16][17][18][19][20][21]. In this picture, after having reviewed the struct and electrochemistry of Fe-S clusters of different nuclearity [10,[22][23][24][25][26][27][28][29][30][31], we now devote attention to the fundamental role of [2Fe-2S] centers in activating a wide spectrum of zymatic reactions. In addition we have reported about the role of prebiotic iron-su peptide catalysts in triggering pH gradients exploited by all known living organisms [ As in our previous papers, this discussion was exclusively limited to those prote whose molecular structure has been ascertained by X-ray crystallography, NMR spect copy, or cryo-electron microscopy.…”

“…In addition we have reported about the role of prebiotic iron-su peptide catalysts in triggering pH gradients exploited by all known living organisms [ As in our previous papers, this discussion was exclusively limited to those prote whose molecular structure has been ascertained by X-ray crystallography, NMR spect copy, or cryo-electron microscopy. (Unless otherwise specified, all images pertinent to molecular architecture of the different species have been obtained by the NGL Viewer Since we have already dealt with structure and electrochemistry of metalloprote hosting "classical" ([Fe2S2](S γ Cys)4) and Rieske-type [Fe2S2](Cys)2(His)2 ferredoxins [23 well as "non-classical" [Fe2S2](Cys)3(X) (X = Asp, Arg, His) [24] ferredoxins, we did consider them herein.…”

Structure of a putative immature form of a Rieske-type iron-sulfur protein in complex with zinc chloride

“…These various roles are thought to be evidence of the significant influences of iron-sulfur clusters on the development and evolution of life 3 , 4 . While various types of iron-sulfur clusters have been discovered as protein cofactors, the rhomboid [2Fe-2S] cluster and the cubane [4Fe-4S] cluster are the most widely observed type 3 , 5 , 6 .…”