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- W1044999225 abstract "The relationship between the structure of the peptide environment and active site chemical properties is of considerable interest in the recent investigations. This chapter presents some examples of such specific relationships, particularly in the case of iron–sulfur proteins, because this class of proteins is distributed widely in living organisms ranging from bacterial cells to mammals. The major function of the proteins is currently known to be electron transfer and the redox catalysis associated with it. Iron–sulfur clusters play a decisive role in these biological electron transfer functions and the binding of such clusters is considered. Extensive model studies on metal sulfide/thiolate complexes have already been performed. A typical structure of a water-soluble globular protein consists of hydrophilic amino acid residues outside and hydrophobic ones inside. The hydrophobic environments support various electrostatic interactions within the protein that plays a crucial role in the enzymatic reaction. The chapter also discusses chelating effects of peptide ligands, [2Fe–2S] plant-type ferredoxin peptide model complexes, and hydrophobic effect of peptide and related ligands. Specific peptides can also serve as mediators for electron passage, and for protection against dioxygen, water, and protons." @default.
- W1044999225 created "2016-06-24" @default.
- W1044999225 creator A5033661039 @default.
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- W1044999225 date "1989-01-01" @default.
- W1044999225 modified "2023-09-26" @default.
- W1044999225 title "Cysteine-Containing Oligopeptide Model Complexes of Iron-Sulfur Proteins" @default.
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- W1044999225 doi "https://doi.org/10.1016/s0898-8838(08)60193-2" @default.
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