منابع مشابه
Recent advances in understanding blue copper proteins
The type 1 (T1) or blue Cu (BC) proteins are a highly studied group of electron transfer (ET) active sites in bioinorganic chemistry. In this review, we cover several more recent results which extend the understanding of the geometric and electronic structure of these interesting Cu ET sites. Spectroscopicmethods in tandemwithdensity functional theory (DFT) and timedependent-DFT (TD-DFT) calcul...
متن کاملRack-induced bonding in blue-copper proteins.
The unique spectroscopic properties of blue-copper centers, i.e. the strong charge-transfer band at approximately 600 nm and the narrow hyperfine coupling in the EPR spectrum, are reviewed. The concept of rack-induced bonding is summarized. The tertiary structure of the protein creates a performed chelating site with very little flexibility, the geometry of which is in conflict with that prefer...
متن کاملInner- and outer-sphere metal coordination in blue copper proteins.
Blue copper proteins (BCPs) comprise classic cases of Nature's profound control over the electronic structures and chemical reactivity of transition metal ions. Early studies of BCPs focused on their inner coordination spheres, that is, residues that directly coordinate Cu. Equally important are the electronic and geometric perturbations to these ligands provided by the outer coordination spher...
متن کاملStructural Features and Biological Functions in Blue Copper Proteins
A new idea that elucidates the electron carrier ability of plastocyanin (and o f azurin) is proposed. It emphasizes the fact that two lobes of the d-orbital. where one unpaired electron of copper (II) ion lies, are not screened by the ligand atoms, which would facilitate the electron transfer between the d-orbital and the redox partners (cytochrom e/ and P-700 in the case of plastocyanin). Seve...
متن کاملElectronic structures of metal sites in proteins and models: contributions to function in blue copper proteins.
Approximately one-half of all known protein crystal structures in the protein data bank (PDB) contain metal ion cofactors, which play vital roles in charge neutralization, structure, and function.1,2 These proteins range in size from 5000-107 Da with the metal ion corresponding to only on the order of 0.1 wt % of the molecule. Yet, for a wide range of these metalloproteins, the metal ion and it...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 1993
ISSN: 0006-3495
DOI: 10.1016/s0006-3495(93)81332-8