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: 3.44

Impact Factor Rankings

2016 Impact Factor Available summer 2017
2014 / 2015 Impact Factor 3.444
2013 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

Additional details

5-year impact 3.45
Cited half-life 8.20
Immediacy index 0.77
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


  • 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

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: A series of new 3d metal complexes with 5-chloro-quinolin-8-ol (ClQ), [Mn(ClQ)2] (1), [Fe(ClQ)3] (2), [Co(ClQ)2(H2O)2] (3), [Ni(ClQ)2(H2O)2] (4), [Cu(ClQ)2] (5), [Zn(ClQ)2(H2O)2] (6), [Mn(ClQ)3]·DMF (7) and [Co(ClQ)3]·DMF·(EtOH)0.35 (8) (DMF = N,N-dimethylformamide), has been synthesized and characterized by elemental analysis, IR spectroscopy and TG-DTA thermal analysis. X-ray structure analysis of 7 and 8 revealed that these molecular complexes contain three chelate ClQ molecules coordinated to the central atoms in a deformed octahedral geometry and free space between the complex units is filled by solvated DMF and ethanol molecules. Antimicrobial activity of 1 – 6 was tested by determining the minimum inhibitory concentration and minimum microbicidal concentration against 12 strains of bacteria and 5 strains of fungi. The intensity of antimicrobial action varies depending on the group of microorganism and can be sorted: 1 > ClQ > 6 > 3/4 > 2 > 5. Complexes 1 – 6 exhibit high cytotoxic activity against MDA-MB, HCT-116 and A549 cancer cell lines. Among them, complex 2 is significantly more cytotoxic against MDA-MB cells than cisplatin at all tested concentrations and is not cytotoxic against control mesenchymal stem cells indicating that this complex seems to be a good candidate for future pharmacological evaluation. Interaction of 1 – 6 with DNA was investigated using UV-VIS spectroscopy, fluorescence spectroscopy and agarose gel electrophoresis. The binding studies indicate that 1 – 6 can interact with CT-DNA through intercalation, complex 2 has the highest binding affinity. Moreover, complexes 1 – 6 inhibit the catalytic activity of topoisomerase I.
    No preview · Article · Oct 2015 · Journal of Inorganic Biochemistry
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    ABSTRACT: Organometallic complexes have the potential to behave as catalytic drugs. We investigate here Rh(III) complexes of general formula [(Cpx)Rh(N,N′)(Cl)], where N,N′ is ethylenediamine (en), 2,2′-bipyridine (bpy), phenanthroline (phen) or N-(2-aminoethyl)-4-(trifluoromethyl)benzenesulfonamide (TfEn), and Cpx is pentamethylcyclopentadienyl (Cp*), 1-phenyl-2,3,4,5-tetramethylcyclopentadienyl (CpxPh) or 1-biphenyl-2,3,4,5-tetramethyl cyclopentadienyl (CpxPhPh). These complexes can reduce NAD+ to NADH using formate as an hydride source under biologically-relevant conditions. The catalytic activity decreased in the order of N,N-chelated ligand bpy>phen > en with Cp* as the η5-donor. The en complexes (1–3) became more active with extension to the CpX ring, whereas the activity of the phen (7–9) and bpy (4–6) compounds decreased. Cp*Rh(bpy)Cl]+ (4) showed the highest catalytic activity, with a TOF of 37.4±2h−1. Fast hydrolysis of the chlorido complexes 1–10 was observed by 1H NMR (< 10min at 310K). The pKa* values for the aqua adducts were determined to be ca. 8–10. Complexes 1–9 also catalysed the reduction of pyruvate to lactate using formate as the hydride donor. The efficiency of the transfer hydrogenation reactions was highly dependent on the nature of the chelating ligand and the Cpx ring. Competition reactions between NAD+ and pyruvate for reduction by formate catalysed by 4 showed a preference for reduction of NAD+. The antiproliferative activity of complex 3 towards A2780 human ovarian cancer cells increased by up to 50% when administered in combination with non-toxic doses of formate, suggesting that transfer hydrogenation can induce reductive stress in cancer cells.
    Full-text · Article · Oct 2015 · Journal of Inorganic Biochemistry

  • No preview · Article · Oct 2015 · Journal of Inorganic Biochemistry
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    ABSTRACT: [Ru(η6-p-cym)Cl{dpa(CH2)4COOEt}][PF6] (cym = cymene; dpa = 2,2’-dipyridylamine; complex 2) was prepared and characterized by elemental analysis, IR and multinuclear NMR spectroscopy, as well as ESI-MS and X-ray structural analysis. The structural analog without a side chain [Ru(η6-p-cym)Cl(dpa)][PF6] (1) as well as 2 were investigated in vitro against 518A2, SW480, 8505C, A253 and MCF-7 cell lines. Complex 1 is active against all investigated tumor cell lines while the activity of compound 2 is limited only to caspase 3 deficient MCF-7 breast cancer cells, however, both are less active than cisplatin. As CD4+ Th cells are necessary to trigger all the immune effector mechanisms required to eliminate tumor cells, besides testing the in vitro antitumor activity of 1 and 2, the effect of ruthenium(II) complexes on the cells of the adaptive immune system have also been evaluated. Importantly, complex 1 applied in concentrations which were effective against tumor cells did not affect immune cell viability, nor did exert a general immunosuppressive effect on cytokine production. Thus, beneficial characteristics of 2 might contribute to the overall therapeutic properties of the complex.
    No preview · Article · Sep 2015 · Journal of Inorganic Biochemistry
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    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.
    No preview · Article · Jul 2015 · Journal of Inorganic Biochemistry