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301 Newest Publications in journal of biological inorganic chemistry
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Why is the molybdenum-substituted tungsten-dependent formaldehyde ferredoxin oxidoreductase not active? A quantum chemical study
27-11-2012 | Rong-Zhen Liao, Journal of Biological Inorganic Chemistry, 2012
Formaldehyde ferredoxin oxidoreductase is a tungsten-dependent enzyme that catalyzes the oxidative degradation of formaldehyde to formic acid. The molybdenum ion can be incorporated into the active site to displace the tungsten ion, but is without activity. Density functional calculations ...
Contribution of intracellular ATP to cisplatin resistance of tumor cells
27-11-2012 | Verena Schneider, Michaela L. Krieger, Gerd Bendas, Ulrich Jaehde, Ganna V. Kalayda, Journal of Biological Inorganic Chemistry, 2012
Decreased cellular accumulation of cisplatin is a frequently observed mechanism of resistance to the drug. Beside passive diffusion, several cellular proteins using ATP hydrolysis as an energy source are assumed to be involved in cisplatin transport in and out of the cell. This investigation ...
The biochemical effect of Ser166 phosphorylation on Euplotes octocarinatus centrin
26-11-2012 | Ya-Qin Zhao, Jun Yan, Jian-Bin Chao, Ai-Hhua Liang, Bin-Sheng Yang, Journal of Biological Inorganic Chemistry, 2012
Abstract Centrin is a member of the EF-hand superfamily that is phosphorylated during mitosis and is associated with alterations of contractile fibers. To obtain insight into the structural basis for the functional effects of phosphorylation, we found that the serine residue at position 166 ...
Titanium mineralization in ferritin: a room temperature nonphotochemical preparation and biophysical characterization
26-11-2012 | Fairland F. Amos, Kathryn E. Cole, Rachel L. Meserole, Jean P. Gaffney, Ann M. Valentine, Journal of Biological Inorganic Chemistry, 2012
The incremental addition of titanium(III) citrate to H-chain homopolymers of human ferritin results in the formation of 1.5–6.5-nm particles of amorphous TiO2 within the nanocage of the protein. The mineralization conditions are mild, featuring ambient temperature and no need for ...
Elucidating the mechanism of ferrocytochrome c heme disruption by peroxidized cardiolipin
19-11-2012 | Andrej Musatov, Marian Fabian, Rastislav Varhač, Journal of Biological Inorganic Chemistry, 2012
The interaction of peroxidized cardiolipin with ferrocytochrome c induces two kinetically and chemically distinct processes. The first is a rapid oxidation of ferrocytochrome c, followed by a slower, irreversible disruption of heme c. The oxidation of ferrocytochrome c by peroxidized ...
Characterizing the effects of the protein environment on the reduction potentials of metalloproteins
15-11-2012 | Bradley Scott Perrin Jr., Toshiko Ichiye, Journal of Biological Inorganic Chemistry, 2012
The reduction potentials of electron transfer proteins are critically determined by the degree of burial of the redox site within the protein and the degree of permanent polarization of the polypeptide around the redox site. Although continuum electrostatics calculations of protein structures ...
Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin
07-11-2012 | Anthony Bocahut, Valérie Derrien, Sophie Bernad, Pierre Sebban, Sophie Sacquin-Mora, Eric Guittet, Ewen Lescop, Journal of Biological Inorganic Chemistry, 2012
Neuroglobin (Ngb) is a globin present in the brain and retina of mammals. This hexacoordinated hemoprotein binds small diatomic molecules, albeit with lower affinity compared with other globins. Another distinctive feature of most mammalian Ngb is their ability to form an internal disulfide ...
Fe–O versus O–O bond cleavage in reactive iron peroxide intermediates of superoxide reductase
07-11-2012 | Amr Ali Ahmed Ali Attia, Daniela Cioloboc, Alexandru Lupan, Radu Silaghi-Dumitrescu, Journal of Biological Inorganic Chemistry, 2012
It is generally accepted that the catalytic cycles of superoxide reductases (SORs) and cytochromes P450 involve a ferric hydroperoxo intermediate at a mononuclear iron center with a coordination sphere consisting of four equatorial nitrogen ligands and one axial cysteine thiolate trans to the ...
Protein metalation by metal-based drugs: reactions of cytotoxic gold compounds with cytochrome c and lysozyme
06-11-2012 | Chiara Gabbiani, Lara Massai, Federica Scaletti, Elena Michelucci, Laura Maiore, Maria Agostina Cinellu, Luigi Messori, Journal of Biological Inorganic Chemistry, 2012
Protein metalation processes are crucial for the mechanism of action of several anticancer metallodrugs and warrant deeper characterisation. We have explored the reactions of three cytotoxic gold(III) compounds—namely [(bipy2Me)2Au2(μ-O)2][PF6]2 (where bipy2Me is ...
Erratum to: Assignment of the 1H NMR resonances of protein residues in close proximity to the heme of the nitrophorins: similarities and differences among the four proteins from the saliva of the adult blood-sucking insect Rhodnius prolixus
05-11-2012 | Tatiana K. Shokhireva, F. Ann Walker, Journal of Biological Inorganic Chemistry, 2012
Erratum to: Assignment of the 1H NMR resonances of protein residues in close proximity to the heme of the nitrophorins: similarities and differences among the four proteins from the saliva of the adult blood-sucking insect Rhodnius prolixus Content Type Journal Article Category ...
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