Journal of Inorganic Biochemistry (J INORG BIOCHEM)

Publisher: Elsevier

Journal description

Journal of Inorganic Biochemistry publishes research papers and short communications in the following areas: the chemistry, structure, and function of metalloenzymes; the interaction of inorganic ions and molecules with proteins and nucleic acids; the preparation and properties of coordination complexes of biological interest including both structural and functional model systems; the role of metal-containing systems in the regulation of gene expression; the application of spectroscopic methods to determine the structure of metallobiomolecules; the function of trace elements in living systems; and related subjects.

Current impact factor: 3.27

Impact Factor Rankings

2015 Impact Factor Available summer 2015
2013 / 2014 Impact Factor 3.274
2012 Impact Factor 3.197
2011 Impact Factor 3.354
2010 Impact Factor 3.317
2009 Impact Factor 3.252
2008 Impact Factor 3.133
2007 Impact Factor 3.663
2006 Impact Factor 2.654
2005 Impact Factor 2.423
2004 Impact Factor 2.225
2003 Impact Factor 2.343
2002 Impact Factor 2.204
2001 Impact Factor 1.729
2000 Impact Factor 1.46
1999 Impact Factor 1.463
1998 Impact Factor 1.162
1997 Impact Factor 1.342
1996 Impact Factor 1.459
1995 Impact Factor 1.399
1994 Impact Factor 1.478
1993 Impact Factor 1.405
1992 Impact Factor 1.361

Impact factor over time

Impact factor
Year

Additional details

5-year impact 3.43
Cited half-life 7.30
Immediacy index 0.67
Eigenfactor 0.01
Article influence 0.72
Website Journal of Inorganic Biochemistry website
Other titles Journal of inorganic biochemistry (Online)
ISSN 0162-0134
OCLC 39039411
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Elsevier

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Authors pre-print on any website, including arXiv and RePEC
    • Author's post-print on author's personal website immediately
    • Author's post-print on open access repository after an embargo period of between 12 months and 48 months
    • Permitted deposit due to Funding Body, Institutional and Governmental policy or mandate, may be required to comply with embargo periods of 12 months to 48 months
    • Author's post-print may be used to update arXiv and RepEC
    • Publisher's version/PDF cannot be used
    • Must link to publisher version with DOI
    • Author's post-print must be released with a Creative Commons Attribution Non-Commercial No Derivatives License
    • Publisher last reviewed on 03/06/2015
  • Classification
    ​ green

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: Four new cationic Pd(II) and Pt(II) 5,5-diethylbarbiturate (barb) complexes, [M(barb)(bpma)]X•H2O [M = PdII, X = Cl (1); M = PtII, X = NO3− (2)] and [M(barb)(terpy)]NO3•0.5H2O [M = PdII (3); M = PtII (4)], where bpma = bis(2-pyridylmethyl)amine and terpy = terpyridine, were synthesized and characterized by elemental analysis, IR, UV−vis, NMR, ESI-MS and X-ray crystallography. The DNA binding properties of the cationic complexes were investigated by spectroscopic titrations, displacement experiments, viscosity, DNA melting and electrophoresis measurements. The results revealed that the complexes effectively bind to FS-DNA (fish sperm DNA) via intercalative/minor groove binding modes with intrinsic binding constants (Kb) in the range of 0.50 × 104–1.67 × 105 M−1. Absorption, emission and synchronous fluorescence measurements showed strong association of the complexes with protein (BSA) through a static mechanism. The mode of interaction of complexes towards DNA and protein was also supported by molecular docking. Complexes 1 and 3 showed significant nuclear uptake in HT-29 cells. In addition, 1 and 3 showed higher inhibition than cisplatin on the growth of MCF-7 and HT-29 cells and induced apoptosis on these cells much more effectively than the rest of the complexes as evidenced by pyknotic nuclear morphology. The levels of caspase-cleaved cytokeratin 18 (M30 antigen) in HT-29 cells treated with 1 and 3 increased in a dose-dependent manner, suggesting apoptosis. Moreover, qRT-PCR experiments showed that 1 and 3 caused significant increases in the expression of TNFRSF10B in HT-29 cells, indicating the initiation of apoptosis via cell surface death receptors.
    Journal of Inorganic Biochemistry 11/2015; 152:38-52. DOI:10.1016/j.jinorgbio.2015.08.026
  • [Show abstract] [Hide abstract]
    ABSTRACT: Tissues for the study were obtained intraoperatively during hip replacement procedures from 96 patients. In all the cases, the indication for this treatment were primary or secondary degenerative changes in the hip joint. The subject of the study was the head and neck of the femur, resected in situ. Aluminium concentrations measured in femoral head and neck samples from patients aged between 25 and 91 were varied. Statistical methods were applied to determine the variations in relation to the parameters from the background survey. Significant differences in the aluminium content of femoral head samples were observed between patients under and over 60 years of age. Based on the results, it was confirmed that the aluminium accumulates in bones over a lifetime. The study showed that the content of aluminium in the head and neck of the femur depends on the factors such as: type of medicines taken, contact with chemicals at work, differences in body anatomy and sex. The study on the levels of aluminium in bones and the factors affecting its concentration is a valuable source of information for further research on the role of aluminium in bone diseases. Based on the investigations, it was found that the GF-AAS technique is the best analytical tool for routine analysis of aluminium in complex matrix samples. The use of femoral heads in the investigations was approved by the Bioethics Committee of the University of Medical Sciences in Poznań (Poland).
    Journal of Inorganic Biochemistry 08/2015; DOI:10.1016/j.jinorgbio.2015.08.019
  • [Show abstract] [Hide abstract]
    ABSTRACT: Electrogenerated chemiluminescence, ECL, reactions between tris(2,2'-bipyridine)ruthenium(II), [Ru(bpy)3](2+), and PAMAM GX.0 (X=1 and 2) dendrimers in an aqueous medium were carried out at pH10 (fully deprotonated dendrimer surface). ECL was detected in the presence of GX.0 dendrimers without addition of any known coreactant. Atomic force microscopy, AFM, measurements for GX.0 dendrimers in the presence of the [Ru(bpy)3](2+) complex were also done. AFM images showed the existence of aggregates (pillars) of globular shape, as well as interdendrimer networks forming fibers in the x-y direction for dendrimer aqueous solutions. ECL and AFM results in cooperation suggest that the coreactant effect of the end amine groups is improved by both the dendritic branched shells and the globular z-type aggregates. The ECL efficiency trends as a function of [GX.0] (whole range) can be interpreted taking into account the coreactant effect modulated by the presence of the z and x-y type aggregates. Importantly, ECL efficiency values can be taken as a measure of the change induced on the dendrimer aggregation in aqueous solutions when their concentrations rise. Redox potentials of the [Ru(bpy)3](3+/2+) couple in the presence of the G1.0 and G2.0 dendrimers were also determined. Copyright © 2015 Elsevier Inc. All rights reserved.
    Journal of Inorganic Biochemistry 07/2015; DOI:10.1016/j.jinorgbio.2015.06.021
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    ABSTRACT: The complexity and multifactorial nature of neurodegenerative diseases turn quite difficult the development of adequate drugs for their treatment. Multi-target analogues, in conjugation with natural moieties, have been developed in order to combine acetylcholinesterase (AChE) inhibition with antioxidant properties, metal-binding capacity and inhibition of amyloid-β (Aβ) aggregation. Due to the recent interest on natural-based drugs and also the importance of studying the role of transition metal ions in the disease process, we herein evaluate the copper chelating capacity and inhibitory ability for self- and Cu-induced Aβ1-42 aggregation of two nature-base hybrid model compounds obtained from conjugation of a tacrine moiety with a S-allylcystein (1) or S-propargylcystein (2) moiety. Both compounds show a moderate chelating power towards Cu(II) (pCu 7.13-7.51, CL/CCu=10, CCu=10(-6)M, pH7.4), with predominant formation of 1:1 complex species (CuL, CuH-1L) for which the coordination sphere involves the N-amide and the NH2 amine of the cysteine derivative as well as the NH of tacrine. The compounds are able to improve the inhibition of Aβ aggregation in the presence of Cu(II) and this is slightly more relevant for the allyl derivative (1), a stronger copper chelator, than for the propargyl (2). Moreover, the presence of a chloro atom in the tacrine moiety and the size of the chain length between the two NH groups appeared also to improve the inhibition capacity for Aβ aggregation. Copyright © 2015 Elsevier Inc. All rights reserved.
    Journal of Inorganic Biochemistry 06/2015; DOI:10.1016/j.jinorgbio.2015.06.008
  • [Show abstract] [Hide abstract]
    ABSTRACT: In the emerging issue of enhanced multi-resistant properties in infectious pathogens, new nanomaterials with optimally efficient antibacterial activity and lower toxicity than other species attract considerable research interest. In an effort to develop such efficient antibacterials, we a) synthesized acid-catalyzed silica-gel matrices, b) evaluated the suitability of these matrices as potential carrier materials for controlled release of ZnSO4 and a new Zn(II) binary complex with a suitably designed well-defined Schiff base, and c) investigated structural and textural properties of the nanomaterials. Physicochemical characterization of the (empty-loaded) silica-nanoparticles led to an optimized material configuration linked to the delivery of the encapsulated antibacterial zinc load. Entrapment and drug release studies showed the competence of hybrid nanoparticles with respect to the a) zinc loading capacity, b) congruence with zinc physicochemical attributes, and c) release profile of their zinc load. The material antimicrobial properties were demonstrated against Gram-positive (Staphylococcus aureus, Bacillus subtilis, Bacillus cereus) and negative (Escherichia coli, Pseudomonas aeruginosa, Xanthomonas campestris) bacteria using modified agar diffusion methods. ZnSO4 showed less extensive antimicrobial behavior compared to Zn(II)-Schiff, implying that the Zn(II)-bound ligand enhances zinc antimicrobial properties. All zinc-loaded nanoparticles were less antimicrobially active than zinc compounds alone, as encapsulation controls their release, thereby attenuating their antimicrobial activity. To this end, as the amount of loaded zinc increases, the antimicrobial behavior of the nano-agent improves. Collectively, for the first time, sol-gel zinc-loaded silica-nanoparticles were shown to exhibit well-defined antimicrobial activity, justifying due attention to further development of antibacterial nanotechnology. Copyright © 2015 Elsevier Inc. All rights reserved.
    Journal of Inorganic Biochemistry 06/2015; DOI:10.1016/j.jinorgbio.2015.06.004
  • [Show abstract] [Hide abstract]
    ABSTRACT: The structures of two stereoisomers of the chiral anion [VO2(N-salicylidene-isoleucinato)]− possessing three centers of chirality, the vanadium atom (configuration A/C) and the isoleucine moiety (configuration R/S on alpha and beta carbons), are presented. The absolute configuration of all available stereosiomers, CSS, ARR, CSR and ARS, was determined by electronic circular dichroism (ECD), which allows distinguishing between diastereomers, and by vibrational circular dichroism (VCD) capable of differentiating between all four stereoisomers. The comparison of experimental VCD and infrared (IR) spectra with simulated spectra for band assignment revealed the IR spectra of the diastereomers differing significantly in the C–H stretching region of the aromatic part in the molecule. Crystallization from binary systems composed of equal ratio of two stereoisomers of isoleucine, unveiled the lower solubility of CSS and ARR stereoisomers, while a longer crystallization time of the CSR and ARS stereoisomers allowed to proceed the vanadium-catalyzed epimerization, leading to the subsequent presence of the CSS and ARR stereoisomers in the product obtained.
    Journal of Inorganic Biochemistry 05/2015; 147:65. DOI:10.1016/j.jinorgbio.2015.01.011
  • [Show abstract] [Hide abstract]
    ABSTRACT: tert-Butyl hydroperoxide (TBHP) stereoselectively oxidizes substituted 4-pentenols, when activated by (ethyl)[cis-(piperidine-2,6-diyl)dimethyl] vanadates. The reaction affords (tetrahydrofuran-2-yl)methanols in up to 89% yield, and in stereoselectivity ranging between moderate (cis:trans=32:68) to excellent (>99:1). Correlating structures of 4-pentenols, differing by substitution at tetragonal and trigonal stereocenters, to configuration of products obtained from oxidative cyclization provides a reaction model explaining the origin of stereoselectivity by (i) intramolecular oxygen atom transfer to (ii) a chair-like folded alkenol, being (iii) hydrogen-bonded to one of the two aminodiolate oxygens of the chelated vanadate, having (iv) substituents in the chair-like transition structure preferentially aligned equatorially. Substituents at trigonal stereocenters improve 2,5-cis- and 2,4-trans-selectivity for oxidative 4-pentenol cyclization in case of (Z)-configuration. An (E)-substituent does not alter selectivity exerted by a terminal (Z)-substituent of similar steric size. Larger (E)-groups increase the fraction of 2,5-trans-cyclized products. The reaction model additionally implements results from vanadium-51 NMR spectroscopy and density functional theory. According to theory, the (dialkoxy)(oxo)vanadium substituent exerts in the preferred end-on conformation almost no effect on structure and bonding of the peroxide group in tert-butylperoxy vanadates. Changing conformation to a higher in energy side-on arrangement puts the vanadate-bound tert-butylperoxy group into a position to serve in a concerted reaction as combined electron acceptor and oxygen atom donor. Copyright © 2015 Elsevier Inc. All rights reserved.
    Journal of Inorganic Biochemistry 04/2015; 147. DOI:10.1016/j.jinorgbio.2015.04.009
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    ABSTRACT: Uncontrolled reactions in biological media are a main obstacle for clinical translation of V-based anti-diabetic or anti-cancer pro-drugs. We investigated the use of controlled-release pharmaceutical formulations to ameliorate this issue with a series of V(V) and (IV) complexes of anionic polysaccharides. Carboxymethyl cellulose, xanthan gum, or alginic acid formulations were prepared by the reactions of [VO4](3-) with one or two molar equivalents of biological reductants, L-ascorbic acid (AA) or L-cysteine (Cys), in the presence of excess polysaccharide at pH~7 or pH~4. XANES studies with the use of a previously developed library of model V(V), V(IV) and V(III) complexes showed that reactions in the presence of AA led mostly to the mixtures of five- and six-coordinate V(IV) species, while the reactions in the presence of Cys led predominantly to the mixtures of five- and six-coordinate V(V) species. The XANES spectra of some of these samples closely matched those reported previously for [VO4](3-) biotransformation products in isolated blood plasma, red blood cells, or cultured adipocytes, which supports the hypothesis that modified polysaccharides are major binders of V(V) and V(IV) in biological systems. Studies by EPR spectroscopy suggested predominant V(IV)-carboxylato binding in complexes with polysaccharides. One of the isolated products (a V(IV)-alginato complex) showed selective release of low-molecular-mass V species at pH~8, but not at pH~2, which makes it a promising lead for the development of V-containing formulations for oral administration that are stable in the stomach, but release the active ingredient in the intestines. Copyright © 2015 Elsevier Inc. All rights reserved.
    Journal of Inorganic Biochemistry 04/2015; 147. DOI:10.1016/j.jinorgbio.2015.03.016