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PubMed1996

Indium (III) and gallium (III) complexes of bis(aminoethanethiol) ligands with different denticities: stabilities, molecular modeling, and in vivo behavior.

Complexes of Ga(III) and In(III) radionuclides are widely used in diagnostic imaging. In this study, the following ligands of denticities 4, 5, and 6 respectively were prepared: N,N'-bis-(2,2-dimethyl-2-mercaptoethyl) ethylenediamine (4SS), 1-carboxy-N-N'-bis(2,2-dimethyl-2- mercaptoethyl)ethylenediamine (5SS), and N,N'-bis(2,2- dimethyl-2-mercaptoethyl)ethylenediamine-N,N'-diacetic acid (6SS). Syntheses of the two new ligands, 5SS and 6SS, are described. Equilibrium constants for their In(III) and Ga(III) complexes were determined by both direct and ligand-competitive potentiometric methods. The formation constant (KML = [ML]/[M][L]) of In(III)--6SS in 0.100 M KNO3 at 25.0 degrees C is 10(39.8), and its pM at physiological pH (7.4 with 100% excess of the ligand) is 30.9. These values are higher than those of any other previous reported ligand for In(III). The stability constants of the complexes of 4SS, 5SS, 6SS, and the analogous ligand EDDASS, N,N'-bis(2-mercaptoethyl) ethylenediamine-N,N'-diacetic acid, which does not contain gem-dimethyl groups, are compared. The thermodynamic stabilities of the In(III) complexes of all ligands except 6SS are greater than those of the corresponding Ga(III) complexes. The presence of the geminal dimethyl groups in 6SS increased the stability of the Ga(III) and In(III) complexes over those of EDDASS. The effects of the gem-dimethyl groups on complex stabilities are explained by molecular modeling. The serum stabilities and biodistributions out to 1 h postinjection of 67/68Ga and 111In chelates of 4SS, 5SS, and 6SS were measured and compared with those of EDDASS. The 67/68Ga- and 111In-ligand complexes with more donor atoms showed were more stable in serum, both in vitro and in vivo. The biodistributions of the 67/68Ga- and 111In-ligand complexes exhibited distinct trends. None of the 67/68Ga- and 111In-chelates demonstrated significant heart or brain uptake. The majority of uptake for all compounds was in the liver and kidney. The degree of clearance through the liver corresponded to the thermodynamic stability of the complex. Correlations between in vivo behavior, molecular modeling data, and thermodynamic stability of the complexes are discussed.

Animals↗

PubMed1996

Aldosterone activates the nuclear pore transporter in cultured kidney cells imaged with atomic force microscopy.

Nuclear pore complexes (NPC), located in the nuclear envelope, functionally connect the cell nucleus with the cytoplasm and serve as a crucial pathway for macromolecule exchange. A Madin-Darby canine kidney (MDCK) clone that resembles principal cells of the collecting duct was shown recently to respond to sustained aldosterone exposure with a significant increase in the NPC number per nucleus. The present study elucidates the molecular nature of the NPC pathway and its regulation by aldosterone applying atomic force microscopy. We imaged individual NPC in situ and searched for a putative so-called transporter in the NPC centre. In aldosterone-depleted cells we found numerous macromolecules docked to individual NPC waiting for translocation into the nucleoplasm (standby mode=inactive pore). In contrast, in aldosterone-treated cells NPC were frequently found free of macromolecules, indicating that the translocation process kept pace with docking under hormone-stimulated conditions (transport mode=active pore). In the NPC centre we detected a ring-like structure with a central invagination. We assume that the ring is the putative transporter and that the invagination is the channel entrance used for translocation of macromolecules. Transporters were found in open and closed configurations. In conclusion, the results provide evidence for the existence of a nuclear transporter as part of the translocation machinery of an individual NPC. Aldosterone increases the activity of the nuclear transporter and thus facilitates steroid-mediated gene expression.

Aldosterone↗

PubMed2006

Platinum(II)-mediated coupling reactions of acetonitrile with the exocyclic nitrogen of 9-methyladenine and 1-methylcytosine. Synthesis, NMR characterization, and X-ray structures of new azametallacycle complexes.

The hydroxo complex cis-[L2Pt(mu-OH)]2(NO3)2, (L = PMePh2, 1a), in CH3CN solution, deprotonates the NH2 group of 9-methyladenine (9-MeAd) to give the cyclic trinuclear species cis-[L2Pt[9-MeAd(-H)]]3(NO3)3, (L = PMePh2, 2a), in which the nucleobase binds the metal centers through the N(1), N(6) atoms. In solution at room temperature, 2a slowly reacts with the solvent to form quantitatively the mononuclear azametallacycle cis-[L2PtNH=C(Me)[9-MeAd(-2H)]]NO3 (L = PMePh2, 3a), containing as anionic ligand the deprotonated form of molecule N-(9-methyl-1,9-dihydro-purin-6-ylidene)-acetamidine. In the same experimental conditions, the hydroxo complex with PPh3 (1b) forms immediately the insertion product 3b. Single-crystal X-ray analyses of 3a and 3b show the coordination of the platinum cation at the N(1) site of the purine moiety and to the N atom of the inserted acetonitrile, whereas the exocyclic amino nitrogen binds the carbon atom of the same CN group. The resulting six-membered ring is slightly distorted from planarity, with carbon-nitrogen bond distances for the inserted nitrile typical of a double bond [C(3)-N(2) = 1.292(7) Angstroms in 3a and 1.279(11) Angstroms in 3b], while the remaining CN bonds of the metallocycle are in the range of 1.335(8)-1.397(10) Angstroms. A detailed multinuclear 1H, 31P, 13C, and 15N NMR study shows that the nitrogen atom of the inserted acetonitrile molecule binds a proton suggesting for 3a,b an imino structure in solution. In DMSO and chlorinated solvents, 3a slowly releases the nitrile reforming the trinuclear species 2a, whereas 3b forms the mononuclear derivative cis-[L2Pt[9-MeAd(-H)]]NO3 (L = PPh3, 4b), in which the adeninate ion chelates the metal center through the N(6) and N(7) atoms. Complex 4b is quantitatively obtained when 1b reacts with 9-MeAd in DMSO and can be easily isolated if the reaction is carried out in CH(2)Cl(2). In CH(3)CN solution, at room temperature, 4b slowly converts into 3b indicating that the insertion of acetonitrile is a reversible process. A similar metal-mediated coupling reaction occurs when 1a,b react with 1-methylcytosine (1-MeCy) in CH(3)CN. The resulting complexes, cis-[L(2)PtNH=C(Me)[1-MeCy(-2H)]]NO3, (L = PMePh2, 5a and PPh3, 5b), contain the deprotonated form of the ligand N-(1-methyl-2-oxo-2,3-dihydro-1H-pyrimidin-4-ylidene)-acetamidine. The X-ray analysis of 5a shows the coordination of the metal at the N(3) site of the pyrimidine cycle and to the nitrogen atom of the acetonitrile, with features of the six-membered metallocycle only slightly different from those found in 3a and 3b. In CD3CN/CH3(13)CN solution complexes 5a,b undergo exchange of the inserted nitrile, while in DMSO or chlorinated solvents they irreversibly release CH3CN to form species not yet fully characterized. No insertion of CH3CN occurs when the hydroxo complexes are stabilized by PMe3 and PMe2Ph.

Acetonitriles↗

PubMed1992

Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes.

In order to obtain a better structural framework for understanding the catalytic mechanism of carbonic anhydrase, a number of inhibitor complexes of the enzyme were investigated crystallographically. The three-dimensional structure of free human carbonic anhydrase II was refined at pH 7.8 (1.54 A resolution) and at pH 6.0 (1.67 A resolution). The structure around the zinc ion was identical at both pH values. The structure of the zinc-free enzyme was virtually identical with that of the native enzyme, apart from a water molecule that had moved 0.9 A to fill the space that would be occupied by the zinc ion. The complexes with the anionic inhibitors bisulfite and formate were also studied at neutral pH. Bisulfite binds with one of its oxygen atoms, presumably protonized, to the zinc ion and replaces the zinc water. Formate, lacking a hydroxyl group, is bound with its oxygen atoms not far away from the position of the non-protonized oxygen atoms of the bisulfite complex, i.e. at hydrogen bond distance from Thr199 N and at a position between the zinc ion and the hydrophobic part of the active site. The result of these and other studies have implications for our view of the catalytic function of the enzyme, since virtually all inhibitors share some features with substrate, product or expected transition states. A reaction scheme where electrophilic activation of carbon dioxide plays an important role in the hydration reaction is presented. In the reverse direction, the protonized oxygen of the bicarbonate is forced upon the zinc ion, thereby facilitating cleavage of the carbon-oxygen bond. This is achieved by the combined action of the anionic binding site, which binds carboxyl groups, the side-chain of threonine 199, which discriminates between hydrogen bond donors and acceptors, and hydrophobic interaction between substrate and the active site cavity. The required proton transfer between the zinc water and His64 can take place through water molecules 292 and 318.

Anions↗

PubMed2003

Synthesis and structural characterization of novel Re(i) tricarbonyl complexes anchored on a phosphinoarylbenzylamine and a phosphinoaryloxazoline generated in situ.

Reduction of the amide or replacement of the hydroxyl by a bromide in 2-(diphenylphosphanyl)-N-(2-hydroxyethyl)benzamide (H2PNO) yielded the compounds 2-(diphenylphosphanyl)-N-(2-hydroxyethyl)benzylamine (H2CH2PNO, 1) and N-(2-bromoethyl)-2-(diphenylphosphanyl)benzamide (HPNBr, 2), respectively. Compound 2 is obtained in low yield and, depending on the reaction conditions, is mixed with starting material or with a product which has been identified as 2-(2-diphenylphosphinophenyl)oxazoline (PPh3oxaz, 3). Compounds 1 and 2 react with (NEt(4))(2)[ReBr(3)(CO)(3)], leading to the complexes [Re(CO)(3)(kappa(2)-H(2)CH(2)PNO)Br] (4) and [Re(CO)(3)(kappa(2)-PPh(3)oxazBr)] (5), fully characterized by (1)H and (31)P NMR spectroscopy and X-ray crystallographic analysis. Complex 5 is the first example of a Re(I) tricarbonyl anchored on a phosphorus-oxazoline ligand, which has been generated during the course of complex formation. In the unexpected and unusual complex 5, the Re atom is stabilized by a bidentate 2-(2-diphenylphosphinophenyl)oxazoline, by a bromide, and by three facially arranged carbonyl groups. In complex 4, the carbonyl groups are also facially coordinated to the metal center and the other three remaining coordination positions are occupied by a bromide and by the bidentate (P, N) ligand 2-(diphenylphosphanyl)-N-(2-hydroxyethyl)benzylamine.

Journal Article↗

PubMed1997

The X-ray structure of the PurR-guanine-purF operator complex reveals the contributions of complementary electrostatic surfaces and a water-mediated hydrogen bond to corepressor specificity and binding affinity.

The purine repressor, PurR, is the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric transcription factor is activated to bind to cognate DNA operator sites by initially binding either of its physiologically relevant, high affinity corepressors, hypoxanthine (Kd = 9.3 microM) or guanine (Kd = 1.5 microM). Here, we report the 2.5-A crystal structure of the PurR-guanine-purF operator ternary complex and complete the atomic description of 6-oxopurine-induced repression by PurR. As anticipated, the structure of the PurR-guanine-purF operator complex is isomorphous to the PurR-hypoxanthine-purF operator complex, and their protein-DNA and protein-corepressor interactions are nearly identical. The former finding confirms the use of an identical allosteric DNA-binding mechanism whereby corepressor binding 40 A from the DNA-binding domain juxtaposes the hinge regions of each monomer, thus favoring the formation and insertion of the critical minor groove-binding hinge helices. Strikingly, the higher binding affinity of guanine for PurR and the ability of PurR to discriminate against 2-oxopurines do not result from direct protein-ligand interactions, but rather from a water-mediated contact with the exocyclic N-2 of guanine, which dictates the presence of a donor group on the corepressor, and the better electrostatic complementarity of the guanine base and the corepressor-binding pocket.

Bacterial Proteins↗

PubMed1985

Infrared study of the interaction between caffeine and hydroxylic derivatives.

The interaction between caffeine and hydroxylic derivatives (phenols, water) has been studied by infrared (IR) spectroscopy in 1,2-dichloroethane. The formation constants, enthalpies, and entropies of complex formation have been determined. The IR spectra in the vOH and vc=o ranges indicate that hydrogen bond formation occurs at the carbonyl functions, approximately 70% of the complexes being formed at the O6 atom. These results are compared with 1,3-dimethyluracil complexes and discussed as a function of the ionization potential of the two oxygen atoms. In the solid hydrate, the spectroscopic results show that the interaction of water takes place on the N9 atom of the imidazole ring in agreement with earlier X-ray results. The different interaction sites in solution and in the solid state are briefly discussed.

Caffeine↗

PubMed2000

Nuclear pores collapse in response to CO2 imaged with atomic force microscopy.

Nuclear pore complexes (NPCs) are the rate-limiting barriers for the exchange of macromolecules (e.g. transcription factors or mRNA) between the nuclear and cytosolic compartments. NPC conformation determines movement of cargo in either direction and thus controls gene expression. ATP and calcium are known to induce an NPC shape change (increase in height and decrease in diameter) indicating pore contraction. Here we report a CO2-induced shape change which is different to the ATP/calcium response. Experiments were performed on the isolated nuclear envelope of Xenopus laevis oocytes. The nuclear envelope was spread on glass and the native cytoplasmic surface was imaged with atomic force microscopy (AFM). The preparation was scanned in a water-saturated 100% O2 atmosphere at room temperature. Exposure to 5% CO2 (95%O2) led over a time course of minutes to a dramatic NPC shape change (decrease in height and decrease in diameter) indicating pore closure. NPCs turned flat and central channel openings virtually disappeared. The CO2 response was only slowly reversible. We conclude that NPCs apparently collapse in response to CO2, a structural change that could lead to the functional isolation of the cell nucleus.

Adenosine Triphosphate↗

PubMed2006

Laser cooling without repumping: a magneto-optical trap for erbium atoms.

We report on a novel mechanism that allows for strong laser cooling of atoms that do not have a closed cycling transition. This mechanism is observed in a magneto-optical trap (MOT) for erbium, an atom with a very complex energy level structure with multiple pathways for optical-pumping losses. We observe surprisingly high trap populations of over 10(6) atoms and densities of over 10(11) atoms cm(-3), despite the many potential loss channels. A model based on recycling of metastable and ground state atoms held in the quadrupole magnetic field of the trap explains the high trap population, and agrees well with time-dependent measurements of MOT fluorescence. The demonstration of trapping of a rare-earth atom such as erbium opens a wide range of new possibilities for practical applications and fundamental studies with cold atoms.

Journal Article↗

PubMed1992

Computer-controlled spot-scan imaging of crotoxin complex crystals with 400 keV electrons at near-atomic resolution.

400 keV electrons yield a better relative image contrast than 100 keV electrons for a beam-sensitive organic crystal when spot-scan imaging is used [J. Brink and W. Chiu, J. Microscopy 161 (1991) 279]. A FORTRAN 77 program has been written to operate the spot-scan imaging system on a computer workstation under the VMS operating system which is interfaced serially to the JEOL4000 electron microscope. We demonstrate the application of this implementation by imaging crotoxin complex crystals embedded in either vitreous ice or glucose to 2.5 A resolution. The intensity strength of the structure factors of this protein crystal are different at low (> 10 A) resolution but similar at high resolution (< 10 A) for the two embedding media as expected from their scattering contrast difference. Based on our experience as judged from the electron diffraction patterns of highly tilted crystals, flat crystals embedded in glucose can be readily obtained. Furthermore, our spot-scan imaging system also has the option of correcting the focus gradient that is present in images of tilted specimens.

Computers↗

PubMed2003

Swift oxo transfer reactions of perchlorate and other substrates catalyzed by rhenium oxazoline and thiazoline complexes.

The reaction kinetics and mechanisms of catalytic oxygen atom transfer (OAT) with rhenium oxazoline and thiazoline complexes are described in this feature article. The striking features of this new family of molecular oxotransferases are their rapid kinetics and their surpassed ability in catalyzing the very difficult reduction of perchlorate by atom transfer. The diverse and competing pathways that make these catalysts efficient and practical have been delineated. Factors that govern the rates of OAT reactions have been elucidated on the basis of substrate variation, substituent and steric effects, subtle changes in the coordination environment, and geometrical transformations. This account also presents comparisons of our abiological OAT catalysis to mechanistically related enzymes and model complexes of molybdenum and tungsten.

Journal Article↗

PubMed1984

Visualization of drug-nucleic acid interactions at atomic resolution. VIII. Structures of two ethidium/dinucleoside monophosphate crystalline complexes containing ethidium: cytidylyl(3'-5') guanosine.

This paper describes two complexes containing ethidium and the dinucleoside monophosphate, cytidylyl(3'-5')guanosine (CpG). Both crystals are monoclinic, space group P2l, with unit cell dimensions as follows: modification 1: a = 13.64 A, b = 32.16 A, c = 14.93 A, beta = 114.8 degrees and modification 2: a = 13.79 A, b = 31.94 A, c = 15.66 A, beta = 117.5 degrees. Each structure has been solved to atomic resolution and refined by Fourier and least squares methods; the first has been refined to a residual of 0.187 on 1,903 reflections, while the second has been refined to a residual of 0.187 on 1,001 reflections. The asymmetric unit in both structures contains two ethidium molecules and two CpG molecules; the first structure has 30 water molecules (a total of 158 non-hydrogen atoms), while the second structure has 19 water molecules (a total of 147 non-hydrogen atoms). Both structures demonstrate intercalation of ethidium between base-paired CpG dimers. In addition, ethidium molecules stack on either side of the intercalated duplex, being related by a unit cell translation along the a axis. The basic feature of the sugar-phosphate chains accompanying ethidium intercalation in both structures is: C3' endo (3'-5') C2' endo. This mixed sugar-puckering pattern has been observed in all previous studies of ethidium intercalation and is a feature common to other drug-nucleic acid structural studies carried out in our laboratory. We discuss this further in this paper and in the accompanying papers.

Binding Sites↗

PubMed2006

Structural and electronic analysis of lanthanide complexes: reactivity may not necessarily be independent of the identity of the lanthanide atom--a DFT study.

Density functional theory calculations were used to study a given complex for the whole series of lanthanide cations: [Ln(C3H5)Cp(OMe)] (1) [Ln = La (Z = 57)-Lu (Z = 71)], the radioactive lanthanide promethium (Z = 61) excepted. Contrary to the common assumptions, the calculations suggested a significant, albeit indirect, contribution of f electrons to bonding. Relativistic effects were considered in the calculations of the bonding energies, as well as in geometry optimizations in both spin-restricted and unrestricted formalisms. The unrestricted orbitals were finally used for the analysis of the charges and the composition of the frontier orbitals. It was confirmed that the ionic character was more pronounced for complexes of the late lanthanides.

Journal Article↗

PubMed2006

Structural studies of Bcl-xL/ligand complexes using 19F NMR.

Fluorine atoms are often incorporated into drug molecules as part of the lead optimization process in order to improve affinity or modify undesirable metabolic and pharmacokinetic profiles. From an NMR perspective, the abundance of fluorinated drug leads provides an exploitable niche for structural studies using 19F NMR in the drug discovery process. As 19F has no interfering background signal from biological sources, 19F NMR studies of fluorinated drugs bound to their protein receptors can yield easily interpretable and unambiguous structural constraints. 19F can also be selectively incorporated into proteins to obtain additional constraints for structural studies. Despite these advantages, 19F NMR has rarely been exploited for structural studies due to its broad lines in macromolecules and their ligand complexes, leading to weak signals in 1H/19F heteronuclear NOE experiments. Here we demonstrate several different experimental strategies that use 19F NMR to obtain ligand-protein structural constraints for ligands bound to the anti-apoptotic protein Bcl-xL, a drug target for anti-cancer therapy. These examples indicate the applicability of these methods to typical structural problems encountered in the drug development process.

Fluorine Compounds↗

PubMed2003

Bis(saccharinato-kappa N)zinc(II) complexes with N,N'-bidentate 2-aminomethylpyridine and 2-aminoethylpyridine.

The structures of trans-bis[2-(aminomethyl)pyridine-kappa(2)N,N']bis(saccharinato-kappa N)zinc(II), [Zn(C(7)H(4)NO(3)S)(2)(C(6)H(8)N(2))(2)], (I), and [2-(aminoethyl)pyridine-kappa(2)N,N']bis(saccharinato-kappa N)zinc(II), [Zn(C(7)H(4)NO(3)S)(2)(C(7)H(10)N(2))], (II), exhibit octa- and tetrahedrally coordinated Zn(II) atoms, respectively. The diamine ligands behave as N,N'-bidentate ligands, while saccharinate (sac) is coordinated through the N atom. In (I), the complex lies about an inversion centre with the Zn atom disordered and displaced by 0.256 (2) A from a centre of symmetry towards a sac N atom. The crystal structure of (I) is stabilized by N-H...O hydrogen bonds and the crystal packing of (II) is determined by hydrogen bonding as well as weak pi-pi stacking interactions between the sac ligands.

Journal Article↗

PubMed2001

[Fe(Phen)(CN)4]-: a versatile building block for the design of heterometallic systems. Crystal structures and magnetic properties of PPh4[Fe(Phen)(CN)4]2H2O and [[Fe(Phen)(CN)4]2M(H2O)2]4H2O [Phen = 1,10-phenanthroline; M = Mn(II) and Zn(II)].

The mononuclear PPh4[Fe(phen)(CN)4]*2H2O (1) complex and the cyanide-bridged bimetallic [[Fe(phen)(CN)4]2M(H2O)2]*4H2O compounds [M = Mn(II) (2) and Zn(II) (3); phen = 1,10-phenanthroline; PPh4 = tetraphenylphosphonium cation] have been synthesized and structurally and magnetically characterized. Complex 1 crystallizes in the monoclinic system, space group P2(1)/c, with a = 9.364(4) A, b = 27.472(5) A, c = 14.301(3) A, beta = 97.68(2) degrees, and Z = 4. Complexes 2 and 3 are isostructural and they crystallize in the monoclinic system, space group P2(1)/n, with a = 7.5292(4) A, b = 15.6000(10) A, c = 15.4081(9) A, beta = 93.552(2) degrees, and Z = 2 for 2 and a = 7.440(1) A, b = 15.569(3) A, c = 15.344(6) A, beta = 93.63(2) degrees, and Z = 2 for 3. The structure of complex 1 is made up of mononuclear [Fe(phen)(CN)4]- anions, tetraphenyphosphonium cations, and water molecules of crystallization. The iron(III) is hexacoordinate with two nitrogen atoms of a chelating phen (2.018(6) and 2.021(6) A for Fe-N) and four carbon atoms of four terminal cyanide groups (Fe-C bond lengths varying in the range 1.906(8)-1.95(1) A) building a distorted octahedron around the metal atom. The structure of complexes 2 and 3 consists of neutral double zigzag chains of formula [[Fe(phen)(CN)4]2M(H2O)2] and crystallization water molecules. The [Fe(phen)(CN)4]- entity of 1 is present in 2 and 3 acting as a bridging ligand toward M(H2O)2 units [M = Mn(II) (2) and Zn(II) (3)] through two cyanide groups in cis positions, the other two cyanide remaining terminal. Two water molecules in trans positions and four cyanide-nitrogen atoms from four [Fe(phen)(CN)4]- units build a distorted octahedral surrounding Mn(II) (2) and Zn(II) (3). The M-O bond lengths are 2.185(3) (2) and 2.105(3) A (3), whereas the M-N bond distances vary in the ranges 2.210(3)-2.258(3) A (2) and 2.112(3)-2.186(3) A (3). The structure of the [Fe(phen)(CN)4]- complex ligand in 2 and 3 is as in 1. The shorter intrachain Fe-M distances through bridging cyano are 5.245(5) and 5.208(5) A in 2 and 5.187(1) and 5.132(1) A in 3. The magnetic properties of 1-3 have been investigated in the temperature range 2.0-300 K. Complex 1 is a low-spin iron(III) complex with an appreciable orbital contribution. The magnetic properties of 3 correspond to the sum of two magnetically isolated spin triplets, the magnetic coupling between the low-spin iron(III) centers through the -CN-Zn-NC- bridging skeleton (iron-iron separation larger than 10.2 A) being negligible. More interestingly, 2 exhibits one-dimensional ferrimagnetic behavior due to the noncompensation of the local interacting spins (S(Mn) = 5/2 and S(Fe) = 1/2) which interact antiferromagnetically through bridging cyano groups. A comparison between the magnetic properties of the isostructural compounds 2 and 3 allow us to check the antiferromagnetic coupling in 2.

Journal Article↗

PubMed1987

Chromotest estimation of SOS functions as a screening method for antitumor platinum complexes.

The chromotest which measures the induction of SOS functions in an Escherichia coli strain bearing the lacZ gene under the sfiA gene control was evaluated as a screening method for platinum complexes with antitumor activity. Four types of complexes were used: (a) those with two nitrogen ligands in cis position and chlorine or carboxylic acid as anionic ligand; (b) four nitrogen atoms surrounding platinum; (c) complexes involving sulphur and amino group of methionine; (d) complexes of tetravalent platinum. The trans-diaminodichloro complex was used as negative control. Groups (b) and (c) were inactive in the chromotest which correlated well with their absence of antitumor activity. Antitumor activity and a positive chromotest also correlated in group (d). In group (a), which includes complexes with well established antitumor activity, the chromotest separated complexes with fast and slow rate of hydrolysis. The results fitted well in the mutation induction test.

Alkaline Phosphatase↗

PubMed1994

Observation of binding and polymerization of Fur repressor onto operator-containing DNA with electron and atomic force microscopes.

The Fur (ferric uptake regulation) protein is a global regulator that, in the presence of Fe2+, represses the expression of a number of iron-acquisition genes and virulence determinants such as toxins. Dark-field electron microscopy of positively stained Fur-DNA complexes in addition to atomic force microscopy allowed direct visualization of Fur interactions with the regulatory regions of aerobactin and hemolysin operons and provided complementary information about the structure of the complexes. According to the DNA used and the protein/DNA ratio, Fur binding to DNA results in partial or total covering of the fragments, indicating that the protein initiates polymerization along the DNA molecules at specific sites. Negative staining of Fur-DNA complexes revealed a well-ordered structure of the polymer suggesting a helical arrangement. Local rigidification of the DNA molecules resulting from Fur binding could be involved in the repression process.

Bacterial Proteins↗