The application of voltammetric methods using different rates of polarisation on HMDE reveal inert or labile behaviour of Cd- or Zn- complexes in the presence of excessive cadmium or zinc ions in solution. This
phenomenon was demonstrated first on the simplest phytochelatin &#8211; complex of peptide <mml:math alttext="$\left( {\gamma-{\text{Glu}}-{\text{Cys}}} \right)_2 {\text{Gly}}$" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mrow><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mi>&#947;</mml:mi><mml:mtext>-</mml:mtext><mml:mtext>Glu</mml:mtext><mml:mtext>-</mml:mtext><mml:mtext>Cys</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mn>2</mml:mn></mml:msub><mml:mtext>Gly</mml:mtext></mml:mrow></mml:math> with cadmium, later on rabbit liver metallothioneins &#8211; <mml:math alttext="${\text{Cd}}_{\text{7}} {\text{MT}}$" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msub><mml:mtext>Cd</mml:mtext><mml:mtext>7</mml:mtext></mml:msub><mml:mtext>MT</mml:mtext></mml:math> in the presence of cadmium and <mml:math alttext="${\text{Cd}}_{\text{5}} {\text{Zn}}_2 {\text{MT}}$" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msub><mml:mtext>Cd</mml:mtext><mml:mtext>5</mml:mtext></mml:msub><mml:msub><mml:mtext>Zn</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mtext>MT</mml:mtext></mml:math> in the presence of zinc. Voltammetric methods can distinguish between labile and inert complexes present simultaneously and therefore could elucidate their role in reactions of metal ion transfer.Another method using different rates of polarisation &#8211; elimination voltammetry with linear scan &#8211; proved that S-tetracoordinated complexes of Cd(II) or Zn(II) in the above-mentioned metallothioneins on HMDE are
reduced in the adsorbed state. This implies the possibility of increasing the sensitivity of identification or
determination of the above complexes. On carbon composite electrode, similar behaviour of Cd-complexes
as on HMDE was observed using differential pulse voltammetry.

Ivana  &#352;est&#225;kov&#225;

Tom&#225;&#353;  Navr&#225;til

Voltammetric Methods in Metallothionein Research

In this work we present the synthesis, structural and spectroscopic characterization of Co2+ coordination compounds with ethyl 4-methyl-5-imidazolecarboxylate (emizco). The effects of emizco, the metal salts
<mml:math alttext="${\text{CoCl}}_2 .6{\text{H}}_2 {\text{O}}$" id="E1" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msub><mml:mtext>CoCl</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mn>.6</mml:mn><mml:msub><mml:mtext>H</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mtext>O</mml:mtext></mml:math>, <mml:math alttext="${\text{CoBr}}_2 $" id="E2" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msub><mml:mtext>CoBr</mml:mtext><mml:mn>2</mml:mn></mml:msub></mml:math>, <mml:math alttext="${\text{Co}}\left( {{\text{NO}}_3 } \right)_2 .6{\text{H}}_2 {\text{O}}$" id="E3" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mtext>Co</mml:mtext><mml:msub><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:msub><mml:mrow><mml:mtext>NO</mml:mtext></mml:mrow><mml:mn>3</mml:mn></mml:msub></mml:mrow><mml:mo>)</mml:mo></mml:mrow><mml:mn>2</mml:mn></mml:msub><mml:mn>.6</mml:mn><mml:msub><mml:mtext>H</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mtext>O</mml:mtext></mml:math> and their metal coordination compounds <mml:math alttext="$\left[ {{\text{Co}}\left( {{\text{emizco}}} \right)_{\text{2}} {\text{Cl}}_2 } \right]$" id="E4" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:mtext>Co</mml:mtext><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>emizco</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mtext>2</mml:mtext></mml:msub><mml:msub><mml:mrow><mml:mtext>Cl</mml:mtext></mml:mrow><mml:mn>2</mml:mn></mml:msub></mml:mrow><mml:mo>]</mml:mo></mml:mrow></mml:math>, <mml:math alttext="$\left[ {{\text{Co}}\left( {{\text{emizco}}} \right)_{\text{2}} {\text{Br}}_2 } \right]{\text{.H}}_2 {\text{O}}" id="E5" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:mtext>Co</mml:mtext><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>emizco</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mtext>2</mml:mtext></mml:msub><mml:msub><mml:mrow><mml:mtext>Br</mml:mtext></mml:mrow><mml:mn>2</mml:mn></mml:msub></mml:mrow><mml:mo>]</mml:mo></mml:mrow><mml:msub><mml:mtext>.H</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mtext>O</mml:mtext></mml:math>, <mml:math alttext="$\left[ {{\text{Co}}\left( {{\text{emizco}}} \right)_{\text{2}} \left( {{\text{H}}_2 {\text{O}}} \right)_2 } \right]\left( {{\text{NO}}_3 } \right)_2 {\text{.2H}}_2 {\text{O}}$" id="E6" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:mtext>Co</mml:mtext><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>emizco</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mtext>2</mml:mtext></mml:msub><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:msub><mml:mtext>H</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mtext>O</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mn>2</mml:mn></mml:msub></mml:mrow><mml:mo>]</mml:mo></mml:mrow><mml:msub><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:msub><mml:mrow><mml:mtext>NO</mml:mtext></mml:mrow><mml:mn>3</mml:mn></mml:msub></mml:mrow><mml:mo>)</mml:mo></mml:mrow><mml:mn>2</mml:mn></mml:msub><mml:msub><mml:mtext>.2H</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mtext>O</mml:mtext></mml:math> were evaluated on photosynthesis in spinach
chloroplasts. Seed germination and seedling growth of the monocotyledonous species Lolium multiflorum and Triticum aestivum and the dicotyledonous species Trifolium alexandrinum and Physalis ixocarpa were also assayed under the effect of the compounds and salts. The results showed that cobalt(II) salts and their emizco coordination compounds inhibit photosynthetic electron flow and ATP-synthesis, behaving as Hill reaction inhibitors. Coordination compounds are more potent inhibitors than the salts. It was found that the salts target is at the b6f level while the complexes targets are at QB(D1)-protein and b6f level. The QB inhibition site was confirmed by variable chlorophyll a fluorescence yield. On the other hand, emizco inhibits seed germination, root and shoot development, in both weed and crop species. Cobalt(II) coordination compounds are the most effective photosynthesis inhibitors, but they are less potent than emizco in germination and seedling growth, while the metal salts are the least active of all.

Beatriz King-Díaz

Josefina Montes-Ayala

Concepción Escartín-Guzmán

Silvia E. Castillo-Blum

Roberto Iglesias-Prieto

Blas Lotina-Hennsen

Norah Barba-Behrens

Cobalt(II) Coordination Compounds of Ethyl 4-Methyl-5-Imidazolecarboxylate: Chemical and Biochemical Characterization on Photosynthesis and Seed Germination

In an attempt to probe nucleic acid structures, numerous Ru(II) complexes with different ligands have been synthesized and investigated. In this contribution we focus on the DNA-binding properties of
ruthenium(II) complexes containing asymmetric ligands that have attracted little attention in the past decades.
The influences of the shape and size of the ligand on the binding modes, affinity, enantioselectivities and photocleavage of the complexes to DNA are described.

Hui Chao

Liang-Nian Ji

DNA Interactions with Ruthenium(II) Polypyridine Complexes Containing Asymmetric Ligands

Two proteins were purified and preliminarily characterized from the soluble extract of cells (310 g, wet weight) of the aminolytic and peptidolytic sulfate-reducing bacterium Desulfovibrio (D.) aminophilus DSM
12254. The iron-sulfur flavoenzyme adenylylsulfate (adenosine 5&#39;-phosphosulfate, APS) reductase, a key enzyme in the microbial dissimilatory sulfate reduction, has been purified in three chromatographic steps
(DEAE-Biogel A, Source 15, and Superdex 200 columns). It contains two different subunits with molecular masses of 75 and 18 kDa. The fraction after the last purification step had a purity index <mml:math alttext="$\left( {{{{\text{A}}_{278{\text{nm}}} } \mathord{\left/ {\vphantom {{{\text{A}}_{278{\text{nm}}} } {{\text{A}}_{{\text{388nm}}} }}} \right. \kern-\nulldelimiterspace} {{\text{A}}_{{\text{388nm}}} }}} \right)$" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mrow><mml:mrow><mml:msub><mml:mtext>A</mml:mtext><mml:mrow><mml:mn>278</mml:mn><mml:mo>&#8201;</mml:mo><mml:mtext>nm</mml:mtext></mml:mrow></mml:msub></mml:mrow><mml:mo>/</mml:mo><mml:mrow><mml:msub><mml:mtext>A</mml:mtext><mml:mrow><mml:mn>388</mml:mn><mml:mo>&#8201;</mml:mo><mml:mtext>nm</mml:mtext></mml:mrow></mml:msub></mml:mrow></mml:mrow></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:math> of
5.34, which was used for further EPR spectroscopic studies. The D. aminophilus APS reductase is very similar to the homologous enzymes isolated from D. gigas and D. desulfuricans ATCC 27774. A tetraheme
cytochrome <mml:math alttext="$c_3$" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msub><mml:mi>c</mml:mi><mml:mn>3</mml:mn></mml:msub></mml:math> (His-heme iron-His) has been purified in three chromatographic steps (DEAE- Biogel A,
Source 15, and Biogel-HTP columns) and preliminarily characterized. It has a purity index <mml:math alttext="$\left( {{{\left[ {{\text{A}}_{553{\text{nm}}} - {\text{A}}_{570{\text{nm}}} } \right]_{{\text{red}}} } \mathord{\left/ {\vphantom {{\left[ {{\text{A}}_{553{\text{nm}}} - {\text{A}}_{570{\text{nm}}} } \right]_{{\text{red}}} } {{\text{A}}_{280{\text{nm ox}}} }}} \right. \kern-\nulldelimiterspace} {{\text{A}}_{280{\text{nm ox}}} }}} \right)$" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mrow><mml:mrow><mml:msub><mml:mrow><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:msub><mml:mtext>A</mml:mtext><mml:mrow><mml:mn>553</mml:mn><mml:mo>&#8201;</mml:mo></mml:mrow></mml:msub><mml:mtext>-</mml:mtext><mml:msub><mml:mtext>A</mml:mtext><mml:mrow><mml:mn>570</mml:mn><mml:mo>&#8201;</mml:mo></mml:mrow></mml:msub></mml:mrow><mml:mo>]</mml:mo></mml:mrow></mml:mrow><mml:mrow><mml:mtext>red</mml:mtext></mml:mrow></mml:msub></mml:mrow><mml:mo>/</mml:mo><mml:mrow><mml:msub><mml:mtext>A</mml:mtext><mml:mrow><mml:mn>280</mml:mn><mml:mtext>nm</mml:mtext><mml:mo>&#8201;</mml:mo></mml:mrow></mml:msub></mml:mrow></mml:mrow></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:math> of 2.9 and a molecular mass of around 15 kDa, and its spectroscopic characterization
(NMR and EPR) has been carried out. This hemoprotein presents similarities with the tetraheme cytochrome <mml:math alttext="$c_3$" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msub><mml:mi>c</mml:mi><mml:mn>3</mml:mn></mml:msub></mml:math> from Desulfomicrobium (Des.) norvegicum (NMR spectra, and N-terminal amino acid sequence).

Alejandro  L&#243;pez-Cort&#233;s

Sergey  Bursakov

Angelo  Figueiredo

Anders E. Thapper

Smilja  Todorovic

Jos&#233; J. G. Moura

Bernard  Ollivier

Isabel  Moura

Guy  Fauque

Purification and Preliminary Characterization of
Tetraheme Cytochrome <svg style="vertical-align:-3.3907pt" height="11.9625" version="1.1" viewBox="0 0 13.3625 11.9625" width="13.3625" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg"><g transform="matrix(.017,-0,0,-.017,.062,7.675)"><path id="x1D450" d="M383 397q0 -32 -35 -49q-12 -6 -23 8q-37 45 -84 45t-90 -71q-40 -65 -40 -167q0 -57 22 -86t59 -29q38 0 81.5 24.5t69.5 51.5l16 -21q-44 -53 -104 -84t-109 -31q-56 0 -89.5 41t-33.5 117q0 61 30 124t79 105q33 28 81 50.5t86 22.5q34 0 59 -15.5t25 -35.5z" /></g><g transform="matrix(.012,-0,0,-.012,6.962,11.762)"><path id="x33" d="M285 378v-2q65 -13 102 -54.5t37 -97.5q0 -57 -30.5 -104.5t-74 -75t-85.5 -42t-72 -14.5q-31 0 -59.5 11t-40.5 23q-19 18 -16 36q1 16 23 33q13 10 24 0q58 -51 124 -51q55 0 88 40t33 112q0 64 -39 96.5t-88 32.5q-29 0 -64 -11l-6 29q77 25 118 57.5t41 84.5&#xA;q0 45 -26.5 69.5t-68.5 24.5q-67 0 -120 -79l-20 20l43 63q51 56 127 56h1q66 0 107 -37t41 -95q0 -42 -31 -71q-22 -23 -68 -54z" /></g></svg> and Adenylylsulfate Reductase from the Peptidolytic Sulfate-Reducing
Bacterium Desulfovibrio aminophilus DSM 12254

Batch and column experiments were performed to determine the Cu(II) binding capacity of silica-immobilized humin biomass. For column studies, 500 bed volumes of a 0.1 mM Cu(II) solution were passed through humin packed columns at the flow rates of 1, 1.5, 2, and 3 mL/min. The biopolymer showed an average Cu binding capacity of 12 ± 1.5 mg/g and a Cu recovery of about 96.5 % ± 1.5. The breakthrough points for Cu(II) alone were approximately 420, 390, 385, and 300 bed volumes for the flow rates of 1, 1.5, 2 and 3 mL/min, respectively. The interference studies demonstrated that at low concentrations, the hard cations Ca(II) and Mg(II) did not seem to represent a major interference on Cu(II) binding to the humin biopolymer. The selectivity showed by this biopolymer was Cu(II)&gt;Ca(II)&gt;Mg(II). On the other hand, batch experiments showed that Ca(II) + Mg(II) at 100mM each reduced the Cu(II) binding to 73 %. However, 1000 mM concentrations of Ca(II) and Mg(II), separately and in mixture, reduced the Cu(II) binding to 47 %, 44 % and 31 %, respectively. The results of this study showed that immobilized humin in a silica matrix could represent an inexpensive bio-source for Cu removal from contaminated water, even in the presence of low concentrations of the hard cations Ca(II) and Mg(II).

Jorge L. Gardea-Torresdey

Carolina Contreras

Guadalupe de la Rosa

Jose R. Peralta-Videa

Flow Rate and Interference Studies for Copper Binding
to a Silica-Immobilized Humin Polymer Matrix:
Column and Batch Experiments

The incorporation of benzene-l,2-dithiolato building blocks into supramolecular coordination assemblies
is the main objective of the investigations described here. Special interest is directed towards dinuclear
complexes with bis(benzene-l,2-dithiolato) ligands, which might be able to form helical structures.
Bis(benzene-l,2-dithiolato) ligands are accessible by ortho-functionalization and subsequent linkage of two
benzene-l,2-dithiol units. The preparation of well defined complexes of titanium, cobalt and nickel with
bis(benzene-l,2-dithiolato) ligands requires strictly thermodynamic equilibration conditions. In that case the
size and shape of the ligand backbone determine if dinuclear double-stranded or mononuclear chelate
complexes are obtained. The dinuclear double-stranded complexes with Ni(II) and Ni(III) are characterized
by a coplanar non-helical arrangement of the square-planar bis(benzene-l,2-dithiolato)nickelate moieties.
The complete structural characterization of the series <mml:math alttext="$\left[ {{\text{M}}\left( {{\text{C}}_6 {\text{H}}_4 {\text{S}}_2 - 1,2} \right)_3 } \right]^{{\text{n}} - } $" id="E1" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msup><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:mtext>M</mml:mtext><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:msub><mml:mtext>C</mml:mtext><mml:mn>6</mml:mn></mml:msub><mml:msub><mml:mtext>H</mml:mtext><mml:mn>4</mml:mn></mml:msub><mml:msub><mml:mtext>S</mml:mtext><mml:mn>2</mml:mn></mml:msub><mml:mtext>-</mml:mtext><mml:mn>1</mml:mn><mml:mo>,</mml:mo><mml:mn>2</mml:mn></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mn>3</mml:mn></mml:msub></mml:mrow><mml:mo>]</mml:mo></mml:mrow><mml:mrow><mml:mtext>n</mml:mtext><mml:mtext>-</mml:mtext></mml:mrow></mml:msup></mml:math> (n = 0, 1, 2) for molybdenum and
tungsten indicates an interesting coordination chemistry of dinuclear triple-stranded complexes.

Wolfram W. Seidel

F. Ekkehardt Hahn

Chances and Limits of the Coordination Chemistry with
Bis(benzene-l,2-dithiolato) Ligands

This investigation reveals the capability of Agave lechuguilla for trivalent and hexavalent chromium removal from aqueous solutions. Experimentation included pH profile, time dependence, adsorption capacity
(KF and QL), adsorption intensity (<mml:math alttext="$n$" id="E1" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi>n</mml:mi></mml:math> and RL) and saturation capacity (<mml:math alttext="$q_s$" id="E2" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msub><mml:mi>q</mml:mi><mml:mi>s</mml:mi></mml:msub></mml:math>) studies. Batch experiments were conducted at <mml:math alttext="$22^ \circ$" id="E3" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:msup><mml:mn>22</mml:mn><mml:mo>°</mml:mo></mml:msup></mml:math>C to characterize and model the adsorption equilibrium as well as biomass adsorption rates. pH 4 was the optimum for Cr(III) binding, while Cr(VI) optimum binding was at pH 2. Time profile
experiments indicated that the adsorption of Cr(VI) by lechuguilla biomass was time-dependent and that of
Cr(III) was not. Kinetic models demonstrated that a pseudo-second order reaction model best described the
kinetic data for Cr(VI). The adsorption isotherms showed that the binding pattern for Cr(VI) followed the
Freundlich isotherm model, while that for Cr(III) followed the Langmuir isotherm.

Jaime Romero-González

José R. Peralta-Videa

Elena Rodríguez

Determination of Equilibrium and Kinetic Parameters of
the Adsorption of Cr(III) and Cr(VI) from Aqueous
Solutions to Agave Lechuguilla Biomass

The interaction of the diastereomeric complexes Λ- and <mml:math alttext="$\Delta - \left[ {{\text{Ru}}\left( {{\text{bpy}}} \right)_2 \left( {{\text{m}} - {\text{GHK}}} \right)} \right]{\text{Cl}}_2$" id="E3" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi>Δ</mml:mi><mml:mtext>-</mml:mtext><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:mtext>Ru</mml:mtext><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>bpy</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mn>2</mml:mn></mml:msub><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>m</mml:mtext><mml:mtext>-</mml:mtext><mml:mtext>GHK</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mo>]</mml:mo></mml:mrow><mml:msub><mml:mtext>Cl</mml:mtext><mml:mn>2</mml:mn></mml:msub></mml:math>, (GHK = glycine-histidine-lysine) to the deoxynucleotide duplex d(5'-CGCGAATTCGCG-3')2 was studied by means of 1H NMR spectroscopy. The diastereomers interact with the oligonucleotide duplex differently. The <mml:math alttext="$\Delta - \left[ {{\text{Ru}}\left( {{\text{bpy}}} \right)_2 \left( {{\text{m}} - {\text{GHK}}} \right)} \right]{\text{Cl}}_2$" id="E4" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mi>Δ</mml:mi><mml:mtext>-</mml:mtext><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:mtext>Ru</mml:mtext><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>bpy</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mn>2</mml:mn></mml:msub><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>m</mml:mtext><mml:mo>-</mml:mo><mml:mtext>GHK</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mo>]</mml:mo></mml:mrow><mml:msub><mml:mtext>Cl</mml:mtext><mml:mn>2</mml:mn></mml:msub></mml:math> is characterized by major groove binding close to the central part of the
oligonucleotide, with both the peptide and the bipyridine ligand of the complex involved in the binding. The <mml:math alttext="$\Lambda - \left[ {{\text{Ru}}\left( {{\text{bpy}}} \right)_2 \left( {{\text{m}} - {\text{bpy}} - {\text{GHK}}} \right)} \right]{\text{Cl}}_2 $" id="E5" xmlns:mml="http://www.w3.org/1998/Math/MathML"><mml:mrow><mml:mi>Λ</mml:mi><mml:mtext>-</mml:mtext><mml:mrow><mml:mo>[</mml:mo><mml:mrow><mml:mtext>Ru</mml:mtext><mml:msub><mml:mrow><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>bpy</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mn>2</mml:mn></mml:msub><mml:mrow><mml:mo>(</mml:mo><mml:mrow><mml:mtext>m</mml:mtext><mml:mtext>-</mml:mtext><mml:mtext>bpy</mml:mtext><mml:mtext>-</mml:mtext><mml:mtext>GHK</mml:mtext></mml:mrow><mml:mo>)</mml:mo></mml:mrow></mml:mrow><mml:mo>]</mml:mo></mml:mrow><mml:msub><mml:mrow><mml:mtext>Cl</mml:mtext></mml:mrow><mml:mn>2</mml:mn></mml:msub></mml:mrow></mml:math> binds loosely, approaching the helix from the minor groove. The NMR analysis shows that the peptide (GHK) binding has a determinative role in the interactions of both diastereomers with the oligonucleotide.

A. Myari

N. Hadjiliadis

A. Garoufis

1H NMR Study of the Enantioselective Binding of <svg style="vertical-align:-0.0pt" height="11.425" version="1.1" viewBox="0 0 11.7875 11.425" width="11.7875" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg"><g transform="matrix(.017,-0,0,-.017,.062,11.363)"><path id="x39B" d="M671 0h-247v28q49 7 60 18.5t0 45.5l-155 438h-2q-21 -61 -74 -204.5t-75 -210.5q-15 -51 -4.5 -65t67.5 -22v-28h-221v28q50 9 69 26.5t45 84.5l202 517l32 9l194 -535q23 -61 42 -78.5t67 -23.5v-28z"/></g></svg>- and <svg style="vertical-align:-0.0pt" height="11.425" version="1.1" viewBox="0 0 11.025 11.425" width="11.025" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns="http://www.w3.org/2000/svg"><g transform="matrix(.017,-0,0,-.017,.062,11.363)"><path id="x394" d="M600 0h-557v24l268 633l28 8l261 -641v-24zM497 50l-194 489l-196 -489h390z"/></g></svg>-[Ru(bpy)2(m-bpy-GHK)]Cl2 to the DeoxynucleotideDuplex d(5'-C1G2C3G4A5A6T7T8C9G10C11G12-3')2

Heavy metals from mining, smelting operations and other industrial processing facilities pollute
wastewaters worldwide. Extraction of metals from industrial effluents has been widely studied due to the
economic advantages and the relative ease of technical implementation. Consequently, the search for new
and improved methodologies for the recovery of gold has increased. In this particular research, the use of
cone hops biomass (Humulus lupulus) was investigated as a new option for gold recovery. The results
showed that the gold binding to native hops biomass was pH dependent from pH 2 to pH 6, with a maximum
percentage binding at pH 3. Time dependency studies demonstrated that Au(III) binding to native and
modified cone hops biomasses was found to be time independent at pH 2 while at pH 5, it was time
dependent. Capacity experiments demonstrated that at pH 2, esterified hops biomass bound 33.4 mg Au/g of
biomass, while native and hydrolyzed hops biomasses bound 28.2 and 12.0 mg Au/g of biomass,
respectively. However, at pH 5 the binding capacities were 38.9, 37.8 and 11.4 mg of Au per gram of native,
esterified and hydrolyzed hops biomasses, respectively.

M. Laura López

J. L. Gardea-Torresdey

J. R. Peralta-Videa

G. de la Rosa

V. Armendáriz

I. Herrera

H. Troiani

J. Henning

Gold Binding by Native and Chemically Modified
Hops Biomasses

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Bioinorganic Chemistry and Applications publishes research in all aspects of bioinorganic chemistry, including bioorganometallic chemistry and applied bioinorganic chemistry, and applications in fields such as medicine and immunology.

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Chief Editor, Professor Fanizzi, is based at the Università del Salento. His research interests and current projects are related to the study of transition metals (Platinum in particular), coordination organometallic and bioinorganic chemistry, and the applications of high field NMR Spectroscopy.

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Bioinorganic Chemistry and Applications publishes research in all aspects of bioinorganic chemistry, including bioorganometallic chemistry and applied bioinorganic chemistry, and applications in fields such as medicine and immunology.

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Bioinorganic Chemistry and Applications

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