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At least 811 records · Page 45Linked to original sources
PubMed1999

Role of the Invariant Peptide Fragment Forming NH.S Hydrogen Bonds in the Active Site of Cytochrome P-450 and Chloroperoxidase: Synthesis and Properties of Cys-Containing Peptide Fe(III) and Ga(III) (Octaethylporphinato) Complexes as Models.

The primary sequence of Cys-X-Gly-Y- (X, hydrophobic residue; Y, hydrophilic residue) is highly conserved in cytochrome P-450s. The amide NHs of Leu, Gly, and X are assumed to form NH.S hydrogen bonds which are also found in the active site fragment, Cys-Pro-Ala-Leu, of chloroperoxidase (CPO). [Fe(III)(OEP)(Z-cys-Leu-Gly-Leu-OMe)] (OEP, octaethylporphinato; Z, benzyloxycarbonyl) and [Fe(III)(OEP)(Z-cys-Pro-Ala-Leu-OMe)] were synthesized as P-450 and CPO model complexes containing the invariant amino acid fragment of the active site. The corresponding gallium(III) complexes were also synthesized to investigate the solution structures using two-dimensional (2D) NMR experiments because the Ga(III) ion is similar to the Fe(III) ion in the ionic radii and in the coordination geometry. The solution structures of the peptide part of the gallium complexes indicate that the invariant fragments maintain a beta I-turn-like conformation and then form NH.S hydrogen bonds between S(gamma)Cys and NH of the third and fourth amino acid residues. The hydrogen bonds have also been confirmed by the (2)H NMR spectra of N(2)H-substituted Fe(III) peptide complexes. The Fe(III)/Fe(II) redox potentials of the Fe(III) complexes indicate that the NH.S hydrogen bonds in the fragments causes a slight positive shift of the redox potential. The tri- and tetrapeptide Fe(III) complexes containing the invariant fragments of P-450 are kinetically stable at 30 degrees C in CH(2)Cl(2). In contrast, [Fe(III)(OEP)(Z-cys-Leu-OMe)] decomposed to give [Fe(II)(OEP)] (22%) and the corresponding disulfide immediately in CD(2)Cl(2) at 30 degrees C for 1 h. These results indicate that the invariant fragments involving the hydrogen bonds cause the stabilization of the high-spin Fe(III) resting state rather than the positive shift of Fe(III)/Fe(II) redox potential.

Journal Article↗
PubMed2004

Design and synthesis of de novo cytochromes c.

Natural c-type cytochromes are characterized by the consensus Cys-X-X-Cys-His heme-binding motif (where X is any amino acid) by which the heme is covalently attached to protein by the addition of the sulfhydryl groups of two cysteine residues to the vinyl groups of the heme. In this work, the consensus sequence was used for the heme-binding site of a designed four-helix bundle, and the apoproteins with either a histidine residue or a methionine residue positioned at the sixth coordination site were synthesized and reacted with iron protoporphyrin IX (protoheme) under mild reducing conditions in vitro. These polypeptides bound one heme per helix-loop-helix monomer via a single thioether bond and formed four-helix bundle dimers in the holo forms as designed. They exhibited visible absorption spectra characteristic of c-type cytochromes, in which the absorption bands shifted to lower wavelengths in comparison with the b-type heme binding intermediates of the same proteins. Unexpectedly, the designed cytochromes c with bis-His-coordinated heme iron exhibited oxidation-reduction potentials similar to those of their b-type intermediates, which have no thioether bond. Furthermore, the cytochrome c with His and Met residues as the axial ligands exhibited redox potentials increased by only 15-30 mV in comparison with the cytochrome with the bis-His coordination. These results indicate that highly positive redox potentials of natural cytochromes c are not only due to the heme covalent structure, including the Met ligation, but also due to noncovalent and hydrophobic environments surrounding the heme. The covalent attachment of heme to the polypeptide in natural cytochromes c may contribute to their higher redox potentials by reducing the thermodynamic stability of the oxidized forms relatively against that of the reduced forms without the loss of heme.

Amino Acid Sequence↗
PubMed2001

Redox-dependent activation of CO dehydrogenase from Rhodospirillum rubrum.

Studies of initial activities of carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum show that CODH is mostly inactive at redox potentials higher than -300 mV. Initial activities measured at a wide range of redox potentials (0--500 mV) fit a function corresponding to the Nernst equation with a midpoint potential of -316 mV. Previously, extensive EPR studies of CODH have suggested that CODH has three distinct redox states: (i) a spin-coupled state at -60 to -300 mV that gives rise to an EPR signal termed C(red1); (ii) uncoupled states at <-320 mV in the absence of CO(2) referred to as C(unc); and (iii) another spin-coupled state at <-320 mV in the presence of CO(2) that gives rise to an EPR signal termed C(red2B). Because there is no initial CODH activity at potentials that give rise to C(red1), the state (C(red1)) is not involved in the catalytic mechanism of this enzyme. At potentials more positive than -380 mV, CODH recovers its full activity over time when incubated with CO. This reductant-dependent conversion of CODH from an inactive to an active form is referred to hereafter as "autocatalysis." Analyses of the autocatalytic activation process of CODH suggest that the autocatalysis is initiated by a small fraction of activated CODH; the small fraction of active CODH catalyzes CO oxidation and consequently lowers the redox potential of the assay system. This process is accelerated with time because of accumulation of the active enzyme.

Aldehyde Oxidoreductases↗
PubMed2001

Ferrocenoyl amino acids and peptides: probing peptide structure.

Recent studies clearly show the utility of the carbodiimide protocol to attach the redox-active Fc moiety to the N-terminal side of amino acids and peptides under mild conditions, resulting in stable and often crystalline products that afford themselves to structural analysis by X-ray crystallography. Electrochemical studies of Fc-peptides show that there is a significant influence of the redox potential depending on the amino acid sequence. The Fc moiety is sensitive to structural changes that occur in the peptide to which it is attached. For helical Fc-oligoprolines, the redox potential of the Fc group makes it easier to oxidize as the oligoproline chain increases in length. Nonhelical peptides, having a similar primary but different secondary structure, give rise to very different redox potentials. The ramifications of these findings to biological systems are significant in that they provide further evidence that the redox properties of a metal center are influenced by factors that go beyond the primary ligand sphere and thus for the involvement of long-range interactions. The Fc group is clearly sensitive to the shape of the peptide. These effects are currently under more detailed investigation [45] in order to gain further insight into the electronic structure of these ferrocenoyl peptides. Although we are not yet in a position to distinguish between "sensing" coordination or "sensing" conformation changes, this effect is of interest because it may allow the development of peptidic sensors.

Amino Acids↗
PubMedDate not supplied

[Growth and proton-potassium exchange in Enterococcus hirae: protonophore effect and the role of oxidation-reduction potential].

Enterococcus hirae ATCC 9790 are able to grow under anaerobic conditions during the fermentation of sugars (pH 8.0) in the presence of the protonophore carbonylcyanide-m-chlorophenylhydrazone at a lesser specific growth rate. As bacteria grow, the acidification of the external medium and a drop in the redox potential from positive to negative (up to -220 mV) values occur. The reducer dithiothreitol, which maintains the negative values of the redox potential, increases the growth rate and acidification of the medium, recovering thereby the effect of the protonophore (without interacting with it). Conversely, the impermeable oxidizer ferricyanide, while maintaining positive values of the redox potential, inhibits the bacterial growth. These results indicate the role of the proton-motive force and importance of reducing processes in bacterial growth. The proton-potassium exchange is inhibited by carbonylcyanide-m-chlorophenylhydazone but is restored with dithiothreitol. Dithiothreiol is able to substitute the proton-motive force; however, ferricyanide and dithiothreitol may also directly affect the bacterial membrane.

Anaerobiosis↗
PubMed1986

Properties of the complexes of riboflavin 3',5'-bisphosphate and the apoflavodoxins from Megasphaera elsdenii and Desulfovibrio vulgaris.

Megasphaera elsdenii and Desulfovibrio vulgaris apoflavodoxins have been reconstituted with riboflavin 3',5'-bisphosphate. Several biochemical and biophysical properties of the complexes have been investigated and the results are compared with the properties of the native proteins. The dissociation constant of the modified complex of M. elsdenii flavodoxin is increased by a factor of about 23 by comparison with that of the native protein. The rate constant for the formation of the complex of M. elsdenii flavodoxin is about 26 times lower than that for the native protein. The redox potential of the transition between the oxidized and semiquinone state is similar to that of the native protein. On the other hand, the redox potential of the semiquinone-hydroquinone transition is about 20 mV more negative than that of the native protein. Absorbance and circular dichroic spectra of the protein-bound artificial prosthetic group and the protein-bound natural prosthetic group are very similar. In both the oxidized and in the fully reduced state only minor differences in interaction between the isoalloxazine ring and the apoprotein for the two flavin derivatives are found by 13C and 15N NMR. 31P-NMR studies show that the 5'-phosphate group of the two flavin derivatives is bound in the same way and that it is dianionic in the complex. In contrast, the 3'-phosphate group in riboflavin 3',5'-bisphosphate is monoanionic or even neutral when bound to the protein. The 3'-phosphate group is also close to or on the surface of the protein. Desulfovibrio vulgaris apoflavodoxin has an affinity for riboflavin 3',5'-bisphosphate which is 10 times higher as compared to Megasphaera elsdenii apoflavodoxin (Ka = 10(8) M-1). Also the association rate constant of Desulfovibrio vulgaris apoprotein and riboflavin 3'5'-bisphosphate is found to be 10 times faster than for the Megasphaera elsdenii flavodoxin reaction. The dissociation behaviour of native Desulfovibrio vulgaris flavodoxin measured under identical conditions as for the riboflavin 3',5'-bisphosphate analog gives a value (Kd approximately equal to 0.2 nM) which is considerably lower than reported earlier [Dubourdieu, M., MacKnight, M. L. & Tollin, G. (1974) Biochem. Biophys. Res. Commun. 60, 649-655]. The results are discussed in the light of the existing crystallographic data of flavodoxins and the recently proposed theory on the regulation of the redox potential in flavoproteins [Moonen, C. T. W., Vervoort, J. & Müller, F. (1984) in Flavins and flavoproteins, pp. 493-496, Walter de Gruyter, Berlin].

Apoproteins↗
PubMed1990

Modifications of the active center of T4 thioredoxin by site-directed mutagenesis.

The active site sequence of T4 thioredoxin, Cys-Val-Tyr-Cys, has been modified in two positions to Cys-Gly-Pro-Cys to mimic that of Escherichia coli thioredoxin. The two point mutants Cys-Gly-Tyr-Cys and Cys-Val-Pro-Cys have also been constructed. The mutant proteins have similar reaction rates with T4 ribonucleotide reductase as has the wild-type T4 thioredoxin. Mutant T4 thioredoxins with Pro instead of Tyr at position 16 in the active site sequence have three to four times lower apparent KM with E. coli ribonucleotide reductase than wild-type T4 thioredoxin. The KM values for these mutant proteins which do not have Tyr in position 16 are thus closer to E. coli thioredoxin than to the wild-type T4 thioredoxin. The bulky tyrosine side chain probably prevents proper interactions to E. coli ribonucleotide reductase. Also the redox potentials of these two mutant thioredoxins are lower than that of the wild-type T4 thioredoxin and are thereby more similar to the redox potential of E. coli thioredoxin. Mutations in position 15 behave more or less like the wild-type protein. The kinetic parameters with E. coli thioredoxin reductase are similar for wild-type and mutant T4 thioredoxins except that the apparent kcat is lower for the mutant protein with Pro instead of Tyr in position 16. The active site sequence of T4 thioredoxin has also been changed to Cys-Pro-Tyr-Cys to mimic that of glutaredoxins. This change does not markedly alter the reaction rate of the mutant protein with T4 ribonucleotide reductase or E. coli thioredoxin reductase, but the redox potential is lower for this mutant protein than for wild-type T4 thioredoxin.

Amino Acid Sequence↗
PubMed2006

NO removal in continuous BioDeNOx reactors: Fe(II)EDTA2- regeneration, biomass growth, and EDTA degradation.

BioDeNOx is a novel technique for NOx removal from industrial flue gases. In principle, BioDeNOx is based on NO absorption into an aqueous Fe(II)EDTA2- solution combined with biological regeneration of that scrubber liquor in a bioreactor. The technical and economical feasibility of the BioDeNOx concept is strongly determined by high rate biological regeneration of the aqueous Fe(II)EDTA2- scrubber liquor and by EDTA degradation. This investigation deals with the Fe(II)EDTA2- regeneration capacity and EDTA degradation in a lab-scale BioDeNOx reactor (10-20 mM Fe(II)EDTA2-, pH 7.2 +/- 0.2, 55 degrees C), treating an artificial flue gas (1.5 m3/h) containing 60-155 ppm NO and 3.5-3.9% O2. The results obtained show a contradiction between the optimal redox state of the aqueous FeEDTA solution for NO absorption and the biological regeneration. A low redox potential (below -150 mV vs. Ag/AgCl) is needed to obtain a maximal NO removal efficiency from the gas phase via Fe(II)EDTA2- absorption. Fe(III)EDTA- reduction was found to be too slow to keep all FeEDTA in the reduced state. Stimulation of Fe(III)EDTA- reduction via periodical sulfide additions (2 mM spikes twice a week for the conditions applied in this study) was found to be necessary to regenerate the Fe(II)EDTA2- scrubber liquor and to achieve stable operation at redox potentials below -150 mV (pH 7.2 +/- 0.2). However, redox potentials of below -200 mV should be avoided since sulfide accumulation is unwanted because it is toxic for NO reduction. Very low values for biomass growth rate and yield, respectively, 0.043/d and 0.009 mg protein per mg ethanol, were observed. This might be due to substrate limitations, that is the electron acceptors NO and presumably polysulfide, or to physiological stress conditions induced by the EDTA rich medium or by radicals formed in the scrubber upon the oxidation of Fe(II)EDTA2- by oxygen present in the flue gas. Radicals possibly also induce EDTA degradation, which occurs at a substantial rate: 2.1 (+/-0.1) mM/d under the conditions investigated.

Biodegradation, Environmental↗
PubMed1997

Changes in soluble sugar, starch, and alcohol dehydrogenase in Arabidopsis thaliana exposed to N2 diluted atmospheres.

Proper exchange of atmospheric gases is important for normal root and shoot metabolism in plants. This study was conducted to determine how restricted air supply affects foliar carbohydrates, while using the marker enzyme alcohol dehydrogenase (ADH) to report on the oxygenation status of the rootzone. Fourteen-day-old Arabidopsis thaliana (L.) Heynh. plants grown singly in 7-ml tubes containing agarified nutrient medium were placed in coupled Magenta vessels and exposed for six days to either ambient air or one of six different air/nitrogen dilutions. Redox potential of the agar medium was measured immediately after harvesting and freezing leaf tissue, and then root systems were quickly extracted from the agar and frozen for subsequent analyses. Redox potential measurements indicated that this series of gas mixtures produced a transition from hypoxia to anoxia in the root zones. Root ADH activity increased at higher rates as the redox potential neared anoxic levels. In contrast, ADH mRNA expression quickly neared its maximum as the medium became hypoxic and showed little further increase as it became anoxic. Foliar carbohydrate levels increased 1.5- to 2-fold with decreased availability of metabolic gases, with starch increasing at higher concentrations of air than soluble carbohydrate. The results serve as a model for plant performance under microgravity conditions, where absence of convective air movement prevents replenishment of metabolic gases.

Agar↗
PubMed2005

Energetics of primary and secondary electron transfer in Photosystem II membrane particles of spinach revisited on basis of recombination-fluorescence measurements.

Photon absorption by one of the roughly 200 chlorophylls of the plant Photosystem II (PSII) results in formation of an equilibrated excited state (Chl200*) and is followed by chlorophyll oxidation (formation of P680+) coupled to reduction of a specific pheophytin (Phe), then electron transfer from Phe- to a firmly bound quinone (QA), and subsequently reduction of P680+ by a redox-active tyrosine residue denoted as Z. The involved free-energy differences (DeltaG) and redox potentials are of prime interest. Oxygen-evolving PSII membrane particles of spinach were studied at 5 degrees C. By analyzing the delayed and prompt Chl fluorescence, we determined the equilibrium constant and thus free-energy difference between Chl200* and the [Z+,QA-] radical pair to be -0.43+/-0.025 eV, at 10 mus after the photon absorption event for PSII in its S(3)-state. On basis of this value and previously published results, the free-energy difference between P680* and [P680+,QA-] is calculated to be -0.50+/-0.04 eV; the free-energy loss associated with electron transfer from Phe to QA is found to be 0.34+/-0.04 eV. The given uncertainty ranges do not represent a standard deviation or likely error, but an estimate of the maximal error. Assuming a QA-/QA redox potential of -0.08 V, the following redox-potential estimates are obtained: +1.25 V for P680/P680+; +1.21 V for Z/Z+ (at 10 mus); -0.42 V for Phe-/Phe; -0.58 V for P680*/P680+.

Electron Transport↗
PubMed2005

Temporal changes of multiple redox couples from proliferation to growth arrest in IEC-6 intestinal epithelial cells.

Changes in intracellular redox couples and redox reactive molecules have been implicated in the regulation of a variety of cellular processes, including cell proliferation and growth arrest by contact inhibition. However, the magnitude, direction, and temporal relationship of redox changes to cellular responses are incompletely defined. The present work sought to characterize redox and metabolic changes associated with proliferative stages to contact inhibition of growth in rat IEC-6 intestinal epithelial cells. From the first day of culture until 1 day before confluence, an increase in GSH concentrations and a significant reduction in the redox potential of the GSSG/2GSH couple were observed. These changes were accompanied by a decrease in relative reactive oxygen species (ROS) and nitric oxide (NO) concentrations and oxidation of the redox potential of the NADP(+)/reduced NADP and NAD(+)/NADH couples. Postconfluent cells exhibited a significant decrease in GSH concentrations and a significant oxidation of the GSSG/2GSH couple. When cell proliferation decreased, relative ROS concentrations increased (P < 0.01), whereas NO concentrations remained unchanged, and the NAD(+)/NADH couple became more reduced. Together, these data indicate that the redox potential of distinct couples varies differentially in both magnitude and direction during successive stages of IEC-6 growth. This finding points out the difficulty of defining intracellular redox status at particular stages of cell growth by examining only one redox species. In addition, the data provide a numerical framework for future research of regulatory mechanisms governed by distinct intracellular redox couples.

Adenosine Diphosphate↗
PubMed1991

Stepped potential microcoulometry of ferritin.

A coulometric method for measuring the redox potentials of ferritins and the rates of reduction of the iron core is reported. The half-reduction potential, Eo', of the protein is determined from the coulomb-applied potential curve. This curve is obtained from the difference between the curves for the mediator plus protein and the mediator alone. The coulomb-applied potential curves are generated by stepping the potential in increments over the region of interest and measuring the charged passed following each step. The method is reasonably fast, enabling the redox potential to be determined in 1 day, and gives Eo', values for mediators and the protein that are in good agreement with literature values.

Electrochemistry↗
PubMed2004

Cytochrome c550 in the cyanobacterium Thermosynechococcus elongatus: study of redox mutants.

Cytochrome c(550) is one of the extrinsic Photosystem II subunits in cyanobacteria and red algae. To study the possible role of the heme of the cytochrome c(550) we constructed two mutants of Thermosynechococcus elongatus in which the residue His-92, the sixth ligand of the heme, was replaced by a Met or a Cys in order to modify the redox properties of the heme. The H92M and H92C mutations changed the midpoint redox potential of the heme in the isolated cytochrome by +125 mV and -30 mV, respectively, compared with the wild type. The binding-induced increase of the redox potential observed in the wild type and the H92C mutant was absent in the H92M mutant. Both modified cytochromes were more easily detachable from the Photosystem II compared with the wild type. The Photosystem II activity in cells was not modified by the mutations suggesting that the redox potential of the cytochrome c(550) is not important for Photosystem II activity under normal growth conditions. A mutant lacking the cytochrome c(550) was also constructed. It showed a lowered affinity for Cl(-) and Ca(2+) as reported earlier for the cytochrome c(550)-less Synechocystis 6803 mutant, but it showed a shorter lived S(2)Q(B)(-) state, rather than a stabilized S(2) state and rapid deactivation of the enzyme in the dark, which were characteristic of the Synechocystis mutant. It is suggested that the latter effects may be caused by loss (or weaker binding) of the other extrinsic proteins rather than a direct effect of the absence of the cytochrome c(550).

Calcium↗
PubMed2001

Seasonal variations in phosphorus species in the surface sediments of the Gulf of Riga, Baltic Sea.

The redox-dependent variations in concentrations of phosphorus at two different accumulation bottom areas were investigated in the Gulf of Riga (Baltic Sea) between December 1993 and January 1995. The sediment samples from nine sampling occasions were analyzed for phosphorus forms and redox potential. The average concentrations of total phosphorus measured in 0-1 cm (65 and 89 micromol P g(-1) for sites G5 and T3, respectively) were among the highest reported from the entire Baltic Sea. Redox-dependent "mobile" phosphorus (MP) contributed more than 50% of total in the uppermost-oxidized centimeter, whereas in reduced layers it was 16-18% throughout the year. The significant differences (ANOVA, P<0.01) among months of inorganic phosphorus (IP) concentration at 0-1 cm were observed at site G5 due to temporary accumulation of mobile phosphorus mediated by redox-dependent bacteria activity during summer. On the contrary no accumulation was observed at T3 probably as a result of low redox potential caused by high accumulation rates and low bioturbation. Although the water column above sediments remained oxic throughout the investigation period, the redox potential at site T3 was close to the redoxcline (i.e., +230 mV) during summer. Further increase of eutrophication might lead to development of anoxic conditions at sediment-water interface and that in turn will result in rapid release of redox-dependent phosphorus stored in surface sediments. The availability of excess phosphorus will further enhance eutrophication in partly phosphorus-limited Gulf of Riga.

Baltic States↗
PubMed2005

Long-range protein electron transfer observed at the single-molecule level: In situ mapping of redox-gated tunneling resonance.

A biomimetic long-range electron transfer (ET) system consisting of the blue copper protein azurin, a tunneling barrier bridge, and a gold single-crystal electrode was designed on the basis of molecular wiring self-assembly principles. This system is sufficiently stable and sensitive in a quasi-biological environment, suitable for detailed observations of long-range protein interfacial ET at the nanoscale and single-molecule levels. Because azurin is located at clearly identifiable fixed sites in well controlled orientation, the ET configuration parallels biological ET. The ET is nonadiabatic, and the rate constants display tunneling features with distance-decay factors of 0.83 and 0.91 A(-1) in H(2)O and D(2)O, respectively. Redox-gated tunneling resonance is observed in situ at the single-molecule level by using electrochemical scanning tunneling microscopy, exhibiting an asymmetric dependence on the redox potential. Maximum resonance appears around the equilibrium redox potential of azurin with an on/off current ratio of approximately 9. Simulation analyses, based on a two-step interfacial ET model for the scanning tunneling microscopy redox process, were performed and provide quantitative information for rational understanding of the ET mechanism.

Electrochemistry↗
PubMedDate not supplied

[Transformation of p-nitrochlorobenzene by Escherichia coli].

Microorganisms that have not been adapted to p-nitrochlorobenzene (p-NCB) are capable of transforming this compound. Washed cell of Escherichia coli, the resting culture and the homogenate of disintegrated cells transform p-NCB into p-chloroaniline (p-CA). The growing culture of E. coli (Eh = -210 mV) reduces the nitro group of p-NCB. If E. coli cells are separated from the cultural broth under strictly anaerobic conditions, the redox potential rises abruptly (Eh = -110 mV); the filtrate does not transform p-NCB into p-Ca. The rate at which E. coli reduces the nitro group of p-NCB depends on the redox potential of the medium. It is likely that any microorganism is capable of reducing p-NCB at a low value of the redox potential.

Biotransformation↗
PubMed1999

Electrochemical Behavior of the Fe(III) Complexes of the Cyclic Hydroxamate Siderophores Alcaligin and Desferrioxamine E.

The redox behavior of Fe(III) complexes of the cyclic hydroxamate siderophores alcaligin and desferrioxamine E was investigated by cyclic voltammetry. The limiting, pH independent redox potential (E(1/2) vs NHE) is -446 mV for alcaligin above pH 9 and -477 mV for ferrioxamine E above pH 7.5. At lower pH values, the redox potential for both complexes shifts positive, with a loss of voltammetric reversibility which is interpreted to be the consequence of a secondary dissociation of Fe(II) from the reduced form of the complexes. These observations are of biological importance, since they suggest the possibility of a reductive mechanism in microbial cells which utilize these siderophores to acquire Fe. For comparison purposes, cyclic voltammograms were obtained for Fe(III) complexes with trihydroxamic acids of cyclic (ferrioxamine E) and linear (ferrioxamine B) structures, with dihydroxamic acids of cyclic (alcaligin) and linear (rhodotorulic and sebacic acids) structures, and with monohydroxamic acids (acetohydroxamic and N-methylacetohydroxamic acids) at identical conditions. The observed redox potentials allow us to estimate the overall stability constants for fully coordinated Fe(II) complexes as log beta(II)(Fe(2)alcaligin(3)) = 24.6 and log beta(II)(ferrioxamine E) = 12.1. A linear correlation between E(1/2) and pM was found, and the basis for this relationship is discussed in terms of structural (denticity and cyclic/acyclic) and electronic differences among the {alkyl-NOH-CO-alkyl} type of hydroxamic acid ligands studied.

Journal Article↗
PubMed1981

Electron transport across glycerol monooleate bilayer lipid membranes facilitated by magnesium etiochlorin.

The transport of electrons across biological membranes is believed to play an important role in many biophenomena. Although there have been many examples of systems which may be transporting electrons across Mueller-Rudin bilayer lipid membranes (blm), none has been well characterized. The system we describe here comprises a glycerol monooleate blm containing a magnesium etiochlorin (Mg-C) separating two aqueous phases each containing ferricyanide, ferrocyanide, KCl, and a platinum electrode. The E0s for the Mg-C+/Mg-C and ferri-/ferrocyanide couples are 0.22 and 0.24 V vs. SCE. Thus the MG-C+/Mb-C system is easily poised by the ferri-/ferrocyanide system. When the potentials of the ferri-/ferrocyanide couples are different on each side of the blm we show that the open-circuit membrane potential nearly equals the difference between the redox potentials. This is unequivocal evidence that electrons are being transferred across the blm from one aqueous phase to the other. On the basis of these experiments we deduce that electron transport is the major charge transport mechanism. When redox potentials are the same on each side of the blm, the conductance of the membrane can be greater than 10(-3) S/cm2. The conductance is proportional to the second power of the concentration of Mg-C in the membrane-forming mixture. A number of additional experiments are described which attempt to elucidate the mechanism of electron transfer. We believe that our data are consistent with the idea of an electron-hopping mechanism in which the transmembrane electron transport occurs by a series of second-order electron transfers between membrane-bound electron donors (Mg-C) and acceptors (Mg-C+). Alternative explanations are presented.

Electron Transport↗