Bovine Erythrocyte Superoxide Dismutase

Steinman, Howard M.; Naik, V.R.; Abernethy, John Leo; Hill, Robert L.

doi:10.1016/s0021-9258(19)42108-x

Cited by 219 publications

(23 citation statements)

References 53 publications

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“…The two identical active sites containing the metal ions are located 3.4 nm apart. [48][49][50] Copper ion is situated at the bottom of a deep channel bound to three histidines (His-44, His-46, and His-118) and its role is strictly related with the catalytic activity of the enzyme, while zinc ion, important for enzyme stability, is completely buried and bound to two histidines (His-69 and His-78) and to an aspartic acid residue (Asp-81). These two metal ions share an imidazolate ligand (His 61).…”

Section: Discussionmentioning

confidence: 99%

Permethrin and its metabolites affect Cu/Zn superoxide conformation: fluorescence and in silico evidences

et al. 2015

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The proclivity of permethrin and its metabolites to affect the structure and activity of Cu/Zn superoxide dismutase (SOD) has been investigated by using intrinsic fluorescence and 8-ANS fluorescence techniques. In silico molecular docking investigations were carried out in order to assess the means of interaction at a molecular level between SOD and the considered ligands. Results show that both, permethrin and its metabolites are able to induce conformational variation on SOD. Permethrin and 3-phenoxybenzyl alcohol metabolite induce a blue shift toward the hydrophobic amino acids Leu-101, Ile-102, Leu-104, Ile-110 and Ile-111, with a significant peak increase. An opposite effect was shown by 3-phenoxy benzaldehyde and 3-phenoxybenzoic acid with a progressive reduction of tyrosine fluorescence emission, without any shift. Computational findings confirm that all the molecules considered have more than one allosteric binding site but none of them interact with SOD at its catalytic Cu/Zn cleft. Moreover, all the binding poses found are very close in binding energy thus demonstrating that there is not only a preferred interaction site but most of them are important due to their relative energy in equilibrium with a population strictly connected to the ligand concentration. In the obtained complexes, all the ligands are involved in many hydrogen bonds through their polar oxygen moieties but due to the presence of a common aromatic hydrophobic core, many hydrophobic interactions are due to the SOD nature rich in apolar amino acids. Furthermore, for each ligand it can be pointed out the presence of a highly populated docked structure with a specific interaction of permethrin and its metabolites with Tyr-108, responsible for changes in fluorescence emission.

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Section: Discussionmentioning

confidence: 99%

Permethrin and its metabolites affect Cu/Zn superoxide conformation: fluorescence and in silico evidences

et al. 2015

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“…The CuZnSOD enzyme isolated from bovine erythrocytes has been most intensively studied, and both the complete amino acid sequence [ 1 ] and the X-ray structure are known [ 2 ]. The structural analysis of the enzyme has proven that the copper(II) ion is coordinated through four histidine imidazole nitrogens, while the zinc(II) ion is bound through three histidine imidazole nitrogens and the carboxylate group of the aspartic acid.…”

Section: Introductionmentioning

confidence: 99%

The Role of Side Chains in the Fine-Tuning of the Metal-Binding Ability of Multihistidine Peptides

Székely¹,

Csire²,

Balogh³

et al. 2022

Molecules

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The systematic studies of copper(II), nickel(II) and zinc(II) ion complexes of protected multihistidine peptides containing amino acids with different side chains (Ac-SarHAH-NH2, Ac-HADH-NH2, Ac-HDAH-NH2, Ac-HXHYH-NH2 X, Y = A, F, D or K, Ac-HXHAHXH-NH2, X = F or D) have provided information about the metal ion and protein interaction and have made it possible to draw conclusions regarding general trends in the coordination of metal complexes of multihistidine peptides. The stability of the metal complexes significantly depends on the position of the histidines and amino acids, which are present in the neighbourhood of the histidine amino acids as well. The most significant effect was observed on peptides containing aspartic acid or phenylalanine. The redox parameters of complexes, however, depend on the number and position of histidines, and the other side chain donor atoms have practically no effect on the electrochemical properties of imidazole-coordinated species. However, the presence of aspartic acid side chains results in a more distorted geometry of amide-coordinated species and increases the reducibility of these complexes.

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“…From Speier 1993 [210] with permission karyotic tissues [215]. The intracellular form of Cu,Zn-SOD is a homodimeric enzyme with subunits of 16 kD molecular mass and a length of 151 amino acids each (bovine) [32,216]. Each subunit has an active center which contains a Cu 2+ and a Zn 2+ ion [33,217].…”

Section: Superoxide Dismutosesmentioning

confidence: 99%

Evolutionary aspects of copper binding centers in copper proteins

Abolmaali

Taylor

Weser

Structure and Bonding

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A great number of active centers in proteins and enzymes contain transition metals. Each metal imposes specific catalytic properties on the protein which could not be achieved when employing a different metal. The special role and characteristic reactivity of coordinated copper is illustrated by looking at the evolutionary aspects of copper proteins. The evolution of copper-binding sites is closely linked to that of copper proteins. Copper centers have evolved according to various principles, similar to the evolutionary development of proteins and enzymes. Three basic principles may be observed: the copper-binding centers of metallothioneins and type 1 copper centers developed in non-metal proteins; the transformation of the metal-binding centers of iron or manganese proteins led to the development of the type 2 copper centers; and the trinuclear copper-binding centers of the blue oxidases were formed by alterations and recombinations of type 1 copper centers. Simple, although as yet unknown, mononuclear copper centers gave rise to the type 3 copper-binding sites of the hemocyanins and tyrosinases, as well as to the Cu A-and CUB-centers of the cytochrome oxidases and N20reductase. According to this assignment, copper proteins containing either type 1 copper, type 3 copper, CUA-centers, or CUB-centers share a common ancestor. They developed at least in part by divergent evolution. Type 2 copper proteins are the products of convergent evolution and, consequently, show little or no phylogenetic homology.

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Bovine Erythrocyte Superoxide Dismutase

Cited by 219 publications

References 53 publications

Permethrin and its metabolites affect Cu/Zn superoxide conformation: fluorescence and in silico evidences

Permethrin and its metabolites affect Cu/Zn superoxide conformation: fluorescence and in silico evidences

The Role of Side Chains in the Fine-Tuning of the Metal-Binding Ability of Multihistidine Peptides

Evolutionary aspects of copper binding centers in copper proteins

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