Chemical Functions of Single and Double NH—S Hydrogen Bond in Iron-Sulfur Metalloproteins; Model Ligands with Cys-containing Peptide and Simple Acylaminobenzenethiolate

摘要

Metalloenzymes and metalloproteins functioning in biological redox systems contain various transition metal ions surrounded by many Cys thiolate ligands. In the active center of electron transfer metalloproteins having the thiolate ligand, the existence of NH—S hydrogen bond has been proposed by the X-ray crystallographic analysis of some of metalloproteins, e.g. rubredoxins [1], plant-type ferredoxins [2], bacterial ferredoxins [3] and blue-copper proteins [4] as shown in Fig. 1.