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2010
Carvalho, LR, Corvo M, Enugala R, Marques MM, Cabrita EJ.  2010.  Application of HR-MAS NMR in the solid-phase synthesis of a glycopeptide using Sieber amide resin. Magn Reson Chem. 48:323-30., Number 4 AbstractWebsite

The solid-phase synthesis (SPS) of a structurally complex glycopeptide, using Sieber amide resin, was monitored by high resolution magic angle spinning NMR, demonstrating the further application of this technique. A synthetic peptidoglycan derivative, a precursor of a biologically active PGN, known to be involved in the cellular recognition, was prepared by SPS. The synthesis involved the preparation of an N-alloc glucosamine moiety and the synthesis of a simple amino acid sequence L-Ala-D-Glu-L-Lys-D-Ala-D-Ala. Last step consisted the coupling, on solid-phase, of the protected muramyl unit to the peptide chain. Proton spectra with good suppression of the polystyrene signals in swollen resin samples were obtained in DMF-d(7) as a solvent and by using a nonselective 1D TOCSY/DIPSI-2 scheme, thus allowing to follow the SPS without losses of compound and cleavage from the resin. The assignment of the proton spectra of the resin-bound amino acid sequence and of the bound glycopeptide was achieved through the combination of MAS COSY, TOCSY and NOESY.

2009
Ribeiro, MP, Espiga A, Silva D, Baptista P, Henriques J, Ferreira C, Silva JC, Borges JP, Pires E, Chaves P, Correia IJ.  2009.  Development of a new chitosan hydrogel for wound dressing. Wound repair and regeneration. 17(6):817–824., Number 6: Blackwell Publishing Inc AbstractWebsite

Wound healing is a complex process involving an integrated response by many different cell types and growth factors in order to achieve rapid restoration of skin architecture and function. The present study evaluated the applicability of a chitosan hydrogel (CH) as a wound dressing. Scanning electron microscopy analysis was used to characterize CH morphology. Fibroblast cells isolated from rat skin were used to assess the cytotoxicity of the hydrogel. CH was able to promote cell adhesion and proliferation. Cell viability studies showed that the hydrogel and its degradation by-products are noncytotoxic. The evaluation of the applicability of CH in the treatment of dermal burns in Wistar rats was performed by induction of full-thickness transcutaneous dermal wounds. Wound healing was monitored through macroscopic and histological analysis. From macroscopic analysis, the wound beds of the animals treated with CH were considerably smaller than those of the controls. Histological analysis revealed lack of a reactive or a granulomatous inflammatory reaction in skin lesions with CH and the absence of pathological abnormalities in the organs obtained by necropsy, which supported the local and systemic histocompatibility of the biomaterial. The present results suggest that this biomaterial may aid the re-establishment of skin architecture.

Ktonas, PY, Golemati S, Xanthopoulos P, Sakkalis V, Ortigueira MD, Tsekou H, Zervakis M, Paparrigopoulos T, Bonakis A, Economou NT.  2009.  Time?frequency analysis methods to quantify the time-varying microstructure of sleep EEG spindles: Possibility for dementia biomarkers? Journal of Neuroscience Methods. 185:133–142., Number 1 AbstractWebsite

The time-varying microstructure of sleep EEG spindles may have clinical significance in dementia studies and can be quantified with a number of techniques. In this paper, real and simulated sleep spindles were regarded as AM?FM signals modeled by six parameters that define the instantaneous envelope (IE) and instantaneous frequency (IF) waveforms for a sleep spindle. These parameters were estimated using four different methods, namely the Hilbert transform (HT), complex demodulation (CD), matching pursuit (MP) and wavelet transform (WT). The average error in estimating these parameters was lowest for HT, higher but still less than 10% for CD and MP, and highest (greater than 10%) for WT. The signal distortion induced by the use of a given method was greatest in the case of HT and MP. These two techniques would necessitate the removal of about 0.4 s from the spindle data, which is an important limitation for the case of spindles with duration less than 1 s. Although the CD method may lead to a higher error than HT and MP, it requires a removal of only about 0.23 s of data. An application of this sleep spindle parameterization via the CD method is proposed, in search of efficient EEG-based biomarkers in dementia. Preliminary results indicate that the proposed parameterization may be promising, since it can quantify specific differences in IE and IF characteristics between sleep spindles from dementia subjects and those from aged controls.

2008
Baptista, P, Pereira E, Eaton P, c}alo Doria G{\c, Miranda A, Gomes I, Quaresma P, Franco R.  2008.  Gold nanoparticles for the development of clinical diagnosis methods, jun. Analytical and Bioanalytical Chemistry. 391:943–950., Number 3: Springer Abstract

The impact of advances in nanotechnology is particularly relevant in biodiagnostics, where nanoparticle-based assays have been developed for specific detection of bioanalytes of clinical interest. Gold nanoparticles show easily tuned physical properties, including unique optical properties, robustness, and high surface areas, making them ideal candidates for developing biomarker platforms. Modulation of these physicochemical properties can be easily achieved by adequate synthetic strategies and give gold nanoparticles advantages over conventional detection methods currently used in clinical diagnostics. The surface of gold nanoparticles can be tailored by ligand functionalization to selectively bind biomarkers. Thiol-linking of DNA and chemical functionalization of gold nanoparticles for specific protein/antibody binding are the most common approaches. Simple and inexpensive methods based on these bio-nanoprobes were initially applied for detection of specific DNA sequences and are presently being expanded to clinical diagnosis.

Ivanova, GI, Cabrita EJ, O’Connor R, Eustace AJ, Brougham DF.  2008.  Application of diffusion-ordered spectroscopy for the analysis of cancer related biological samples, 2008. Bulgarian Chemical Communications. 40:464-468., Number 4 Abstract

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2007
Fisher, K, Lowe DJ, Tavares P, Pereira AS, Huynh BH, Edmondson D, Newton WE.  2007.  Conformations generated during turnover of the Azotobacter vinelandii nitrogenase MoFe protein and their relationship to physiological function, Nov. Journal Of Inorganic Biochemistry. {101}:{1649-1656}., Number {11-12} Abstract

Various S = 3/2 EPR signals elicited from wild-type and variant Azotobacter vinelandii nitrogenase MoFe proteins appear to reflect different conformations assumed by the FeMo-cofactor with different protonation states. To determine whether these presumed changes in protonation and conformation reflect catalytic capacity, the responses (particularly to changes in electron flux) of the alpha H195Q, alpha H195N, and alpha Q191 K variant MoFe proteins (where His at position 195 in the alpha subunit is replaced by Gln/Asn or Gln at position alpha-191 by Lys), which have strikingly different substrate-reduction properties, were studied by stopped-flow or rapid-freeze techniques. Rapid-freeze EPR at low electron flux (at 3-fold molar excess of wild-type Fe protein) elicited two transient FeMo-cofactor-based EPR signals within 1 s of initiating turnover under N-2 with the alpha H195Q and alpha H195N variants, but not with the alpha Q191K variant. No EPR signals attributable to P cluster oxidation were observed for any of the variants under these conditions. Furthermore, during turnover at low electron flux with the wild-type, alpha H195Q or alpha H195N MoFe protein, the longer-time 430-nm absorbance increase, which likely reflects P cluster oxidation, was also not observed (by stopped-flow spectrophotometry); it did, however, occur for all three MoFe proteins under higher electron flux. No 430-nm absorbance increase occurred with the alpha Q191K variant, not even at higher electron flux. This putative lack of involvement of the P cluster in electron transfer at low electron flux was confirmed by rapid-freeze Fe-57 Mossbauer spectroscopy, which clearly showed FeMo-factor reduction without P cluster oxidation. Because the wild-type, alpha H195Q and alpha H195N MoFe proteins can bind N-2, but alpha Q195K cannot, these results suggest that P cluster oxidation occurs only under high electron flux as required for N-2 reduction. (C) 2007 Elsevier Inc. All rights reserved.

Ferreira, IMPLVO, Eça R, Pinho O, Tavares P, Pereira A, Roque AC.  2007.  Development and Validation of an HPLC/UV Method for Quantification of Bioactive Peptides in Fermented Milks. Journal of Liquid Chromatography & Related Technologies. 30:2139–2147., Number 14 Abstract

The simultaneous separation and quantification of two casein peptides {(IPP}, {VPP)} presenting potent inhibitory activity of angiotensin-converting-enzyme {(ACE)} and casein in fermented milks was developed. Gradient elution was carried out at a flow-rate of 1 {mL/min}, using a mixture of two solvents. Solvent A was 0.1% {TFA} in water and solvent B was acetonitrile-water-trifluoracetic acid 95:5:0.1. The effluent was monitored by {UV} detector at 214 nm. Calibration curves were constructed in the interval of 0.01-1.0 {mg/mL} for {VPP}, 0.005-1.0 {mg/mL} for {IPP}, and 0.05-3.0 {mg/mL} for casein. R2 invariably exceeded 0.999. The detection limits were 0.004 for {VPP}, 0.002 {mg/mL} for {IPP}, and 0.02 {mg/mL} for casein. Repeatability of the method was evaluated by six consecutive injections of two standard solutions containing {VPP}, {IPP}, and casein. The {RSD} values for concentration were all below 5.08%. Recovery studies were carried out to determine the accuracy of the method. Recoveries ranged between 88 and 98.2%. The methodology was applied, not only, for the monitorization of {VPP}, {IPP}, and casein in commercial fermented milks labeled as presenting antihypertensive properties, but also, in milk with different degrees of fermentation by L. Helveticus, and in other commercial functional fermented milks, such as, those presenting cholesterol lowering properties.

Ferreira, IMPLVO, Eca R, Pinho O, Tavares P, Pereira A, Roque AC.  2007.  Development and validation of an HPLC/UV method for quantification of bioactive peptides in fermented milks. JOURNAL OF LIQUID CHROMATOGRAPHY \& RELATED TECHNOLOGIES. {30}:{2139-2147}., Number {13-16} Abstract

The simultaneous separation and quantification of two casein peptides (IPP, VPP) presenting potent inhibitory activity of angiotensin-converting-enzyme (ACE) and casein in fermented milks was developed. Gradient elution was carried out at a flow-rate of 1 mL/min, using a mixture of two solvents. Solvent A was 0.1% TFA in water and solvent B was acetonitrile-water-trifluoracetic acid 95:5:0.1. The effluent was monitored by UV detector at 214 nm. Calibration curves were constructed in the interval of 0.01-1.0 mg/mL for VPP, 0.005-1.0 mg/mL for IPP, and 0.05-3.0 mg/mL for casein. R 2 invariably exceeded 0.999. The detection limits were 0.004 for VPP, 0.002 mg/mL for IPP, and 0.02 mg/mL for casein. Repeatability of the method was evaluated by six consecutive injections of two standard solutions containing VPP, IPP, and casein. The RSD values for concentration were all below 5.08%. Recovery studies were carried out to determine the accuracy of the method. Recoveries ranged between 88 and 98.2%. The methodology was applied, not only, for the monitorization of VPP, IPP, and casein in commercial fermented milks labeled as presenting anti hypertensive properties, but also, in milk with different degrees of fermentation by L Helveticus, and in other commercial functional fermented milks, such as, those presenting cholesterol lowering properties.

2006
de Melo, SJ, Rondao R, Burrows HD, Melo MJ, Navaratnam S, Edge R, Voss G.  2006.  Photophysics of an indigo derivative (keto and leuco structures) with singular properties. Journal of Physical Chemistry A. 110:13653-13661., Number 51 AbstractWebsite
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de Melo, SSJ, Rondao R, Burrows HD, Melo MJ, Navaratnam S, Edge R, Voss G.  2006.  Spectral and photophysical studies of substituted indigo derivatives in their keto forms. Chemphyschem. 7:2303-2311., Number 11 AbstractWebsite
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2004
Pauleta, SR, Cooper A, Nutley M, Errington N, Harding S, Guerlesquin F, Goodhew CF, Moura I, Moura JJ, Pettigrew GW.  2004.  A copper protein and a cytochrome bind at the same site on bacterial cytochrome c peroxidase, Nov 23. Biochemistry. 43:14566-76., Number 46 AbstractWebsite

Pseudoazurin binds at a single site on cytochrome c peroxidase from Paracoccus pantotrophus with a K(d) of 16.4 microM at 25 degrees C, pH 6.0, in an endothermic reaction that is driven by a large entropy change. Sedimentation velocity experiments confirmed the presence of a single site, although results at higher pseudoazurin concentrations are complicated by the dimerization of the protein. Microcalorimetry, ultracentrifugation, and (1)H NMR spectroscopy studies in which cytochrome c550, pseudoazurin, and cytochrome c peroxidase were all present could be modeled using a competitive binding algorithm. Molecular docking simulation of the binding of pseudoazurin to the peroxidase in combination with the chemical shift perturbation pattern for pseudoazurin in the presence of the peroxidase revealed a group of solutions that were situated close to the electron-transferring heme with Cu-Fe distances of about 14 A. This is consistent with the results of (1)H NMR spectroscopy, which showed that pseudoazurin binds closely enough to the electron-transferring heme of the peroxidase to perturb its set of heme methyl resonances. We conclude that cytochrome c550 and pseudoazurin bind at the same site on the cytochrome c peroxidase and that the pair of electrons required to restore the enzyme to its active state after turnover are delivered one-by-one to the electron-transferring heme.

Pessanha, M, Londer YY, Long WC, Erickson J, Pokkuluri PR, Schiffer M, Salgueiro CA.  2004.  Redox Characterization of Geobacter sulfurreducens Cytochrome c7:  Physiological Relevance of the Conserved Residue F15 Probed by Site-Specific Mutagenesis. Biochemistry. 43(30):9909-9917. AbstractWebsite

The complete genome sequence of the δ-proteobacterium Geobacter sulfurreducens reveals a large abundance of multiheme cytochromes. Cytochrome c7, isolated from this metal ion-reducing bacterium, is a triheme periplasmic electron-transfer protein with Mr 9.6 kDa. This protein is involved in metal ion-reducing pathways and shares 56% sequence identity with a triheme cytochrome isolated from the closely related δ-proteobacterium Desulfuromonas acetoxidans (Dac7). In this work, two-dimensional NMR was used to monitor the heme core and the general folding in solution of the G. sulfurreducens triheme cytochrome c7 (PpcA). NMR signals obtained for the three hemes of PpcA at different stages of oxidation were cross-assigned to the crystal structure [Pokkuluri, P. R., Londer, Y. Y., Duke, N. E. C., Long, W. C., and Schiffer, M. (2004) Biochemistry 43, 849−859] using the complete network of chemical exchange connectivities, and the order in which each heme becomes oxidized was determined at pH 6.0 and 8.2. Redox titrations followed by visible spectroscopy were also performed in order to monitor the macroscopic redox behavior of PpcA. The results obtained showed that PpcA and Dac7 have different redox properties:  (i) the order in which each heme becomes oxidized is different; (ii) the reduction potentials of the heme groups and the global redox behavior of PpcA are pH dependent (redox−Bohr effect) in the physiological pH range, which is not observed with Dac7. The differences observed in the redox behavior of PpcA and Dac7 may account for the different functions of these proteins and constitute an excellent example of how homologous proteins can perform different physiological functions. The redox titrations followed by visible spectroscopy of PpcA and two mutants of the conserved residue F15 (PpcAF15Y and PpcAF15W) lead to the conclusion that F15 modulates the redox behavior of PpcA, thus having an important physiological role.

Pokkuluri, PR, Londer YY, Duke NEC, Erickson J, Pessanha M, Salgueiro CA, Schiffer M.  2004.  Structure of a novel c7-type three-heme cytochrome domain from a multidomain cytochrome c polymer. Protein Science. 13(6):1684-1692. AbstractWebsite

The structure of a novel c7-type cytochrome domain that has two bishistidine coordinated hemes and one heme with histidine, methionine coordination (where the sixth ligand is a methionine residue) was determined at 1.7 Å resolution. This domain is a representative of domains that form three polymers encoded by the Geobacter sulfurreducens genome. Two of these polymers consist of four and one protein of nine c7-type domains with a total of 12 and 27 hemes, respectively. Four individual domains (termed A, B, C, and D) from one such multiheme cytochrome c (ORF03300) were cloned and expressed in Escherichia coli. The domain C produced diffraction quality crystals from 2.4 M sodium malonate (pH 7). The structure was solved by MAD method and refined to an R-factor of 19.5% and R-free of 21.8%. Unlike the two c7 molecules with known structures, one from G. sulfurreducens (PpcA) and one from Desulfuromonas acetoxidans where all three hemes are bishistidine coordinated, this domain contains a heme which is coordinated by a methionine and a histidine residue. As a result, the corresponding heme could have a higher potential than the other two hemes. The apparent midpoint reduction potential, Eapp, of domain C is −105 mV, 50 mV higher than that of PpcA.

2003
Unterweissacher, M, Goes J, Paulino N, Evans G, Ortigueira M.  2003.  Efficient Digital Self-Calibration of Video-Rate Pipeline ADCs using White Gaussian Noise, May. IEEE International Symposium on Circuits and Systems. Abstract
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Unterweissacher, M, Goes J, Paulino N, Evans G, Ortigueira M.  2003.  Efficient Digital Self-Calibration of Video-Rate Pipeline ADCs using White Gaussian Noise, May. IEEE International Symposium on Circuits and Systems. Abstract

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Evans, G, Goes J, Steiger-Garção A, Ortigueira MD, Paulino N, Sousa-Lopes J.  2003.  Low-voltage low-power CMOS analogue circuits for Gaussian and uniform noise generation, May. IEEE International Symposium on Circuits and Systems. :145–148. Abstract

A CMOS analogue circuit for Gaussian noise generation as well as a novel circuit for transforming Gaussian noise into uniform noise, both designed for operating with a supply voltage of 1.5V, are presented. Both circuits are optimized for a 0.35 {\ensuremathμ}m standard CMOS technology using an equation-based design methodology based on genetic algorithms. Electrical simulations demonstrate that high noise amplitudes together with reasonable bandwidths can be achieved with relatively low power dissipation. Potential applications include self-calibration and on-chip self-testing of video-rate analogue-to-digital converters.

Evans, G, Goes J, Steiger-Garção A, Ortigueira MD, Paulino N, Sousa-Lopes J.  2003.  Low-voltage low-power CMOS analogue circuits for Gaussian and uniform noise generation, May. IEEE International Symposium on Circuits and Systems. :145–148. Abstract

A CMOS analogue circuit for Gaussian noise generation as well as a novel circuit for transforming Gaussian noise into uniform noise, both designed for operating with a supply voltage of 1.5V, are presented. Both circuits are optimized for a 0.35 {\ensuremathμ}m standard CMOS technology using an equation-based design methodology based on genetic algorithms. Electrical simulations demonstrate that high noise amplitudes together with reasonable bandwidths can be achieved with relatively low power dissipation. Potential applications include self-calibration and on-chip self-testing of video-rate analogue-to-digital converters.

2000
Elisei, F, Lima JC, Ortica F, Aloisi GG, Costa M, Leitao E, Abreu I, Dias A, Bonifacio V, Medeiros J, Macanita AL, Becker RS.  2000.  Photophysical properties of hydroxy-substituted flavothiones. Journal of Physical Chemistry a. 104:6095-6102., Number 25 Abstract
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1999
Bernardo, MA, Pina F, Escuder B, Garcia-Espana E, Godino-Salido ML, Latorre J, Luis SV, Ramirez JA, Soriano C.  1999.  Thermodynamic and fluorescence emission studies on chemosensors containing anthracene fluorophores. Crystal structure of { (CuLCl)-Cl-1 Cl}(2)center dot 2H(2)O L-1 = N-(3-aminopropyl)-N '-3-(anthracen-9-ylmethyl)aminopropylethane-1,2-diamine. Journal of the Chemical Society-Dalton Transactions. :915-921., Number 6 AbstractWebsite
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1998
Pereira, AS, Small W, Krebs C, Tavares P, Edmondson DE, Theil EC, Huynh BH.  1998.  Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization. Biochemistry. {37}:{9871-9876}., Number {28} Abstract

Rapid freeze-quench (RFQ) Mossbauer and stopped-flow absorption spectroscopy were used to monitor the ferritin ferroxidase reaction using recombinant (apo) frog M ferritin; the initial transient ferric species could be trapped by the RFQ method using low iron loading (36 Fe2+/ferritin molecule). Biphasic kinetics of ferroxidation were observed and measured directly by the Mossbauer method; a majority (85%) of the ferrous ions was oxidized at a fast rate of similar to 80 s(-1) and the remainder at a much slower rate of similar to 1.7 s(-1). In parallel with the fast phase oxidation of the Fe2+ ions, a single transient iron species is formed which exhibits magnetic properties (diamagnetic ground state) and Mossbauer parameters (Delta E-Q = 1.08 +/- 0.03 mm/s and delta = 0.62 +/- 0.02 mm/s) indicative of an antiferromagnetically coupled peroxodiferric complex. The formation and decay rates of this transient diiron species measured by the RFQ Mossbauer method match those of a transient blue species (lambda(max) = 650 nm) determined by the stopped-flow absorbance measurement. Thus, the transient colored species is assigned to the same peroxodiferric intermediate. Similar transient colored species have been detected by other investigators in several other fast ferritins (H and M subunit types), such as the human H ferritin and the Escherichia coli ferritin, suggesting a similar mechanism for the ferritin ferroxidase step in all fast ferritins. Peroxodiferric complexes are also formed as early intermediates in the reaction of O-2 With the catalytic diiron centers in the hydroxylase component of soluble methane monooxygenase (MMOH) and in the D84E mutant of the R2 subunit of E. coli ribonucleotide reductase. The proposal that a single protein site, with a structure homologous to the diiron centers in MMOH and R2, is involved in the ferritin ferroxidation step is confirmed by the observed kinetics, spectroscopic properties, and purity of the initial peroxodiferric species formed in the frog M ferritin.

Valentine, AM, Tavares P, Pereira AS, Davydov R, Krebs C, Koffman BM, Edmondson DE, Huynh BH, Lippard SJ.  1998.  Generation of a mixed-valent Fe(III)Fe(IV) form of intermediate Q in the reaction cycle of soluble methane monooxygenase, an analog of intermediate X in ribonucleotide reductase R2 assembly. Journal Of The American Chemical Society. {120}:{2190-2191}., Number {9} Abstract
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Batista, AG, English MJ.  1998.  "Ventricular Late Potential Analysis with Musical and Harmonic Wavelets. Medical Engineering and Physics. 20:773-779. Abstract
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1997
Tavares, P, Pereira AS, Lloyd SG, Danger D, Edmondson DE, Theil EC, Huynh BH.  1997.  Mossbauer spectroscopic and kinetic characterization of ferric clusters formed in h-chain ferritin mineralization.. Abstracts Of Papers Of The American Chemical Society. {213}:{503-INOR}., Number {2} Abstract
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Pereira, AS, Tavares P, Lloyd SG, Danger D, Edmondson DE, Theil EC, Huynh BH.  1997.  Rapid and parallel formation of Fe3+ multimers, including a trimer, during H-type subunit ferritin mineralization. Biochemistry. {36}:{7917-7927}., Number {25} Abstract

Conversion of Fe ions in solution to the solid phase in ferritin concentrates iron required for cell function. The rate of the Fe phase transition in ferritin is tissue specific and reflects the differential expression of two classes of ferritin subunits (H and L). Early stages of mineralization were probed by rapid freeze-quench Mossbauer, at strong fields (up to 8 T), and EPR spectroscopy in an H-type subunit, recombinant frog ferritin; small numbers of Fe (36 moles/mol of protein) were used to increase Fe3+ in mineral precursor forms, At 25 ms, four Fe3+-oxy species (three Fe dimers and one Fe trimer) were identified, These Fe3+-oxy species were found to form at similar rates and decay subsequently to a distinctive superparamagentic species designated the `'young core.'' The rate of oxidation of Fe2+ (1026 s(-1)) corresponded well to the formation constant for the Fe3+- tyrosinate complex (920 s(-1)) observed previously [Waldo, G. S., \& Theil, E. C. (1993) Biochemistry 32, 13261] and, coupled with EPR data, indicates that several or possibly all of the Fe3+-oxy species involve tyrosine. The results, combined with previous Mossbauer studies of Y30F human H-type ferritin which showed decreases in several Fe3+ intermediates and stabilization of Fe2+ [Bauminger, E. R., et al. (1993) Biochem, J. 296, 709], emphasize the involvement of tyrosyl residues in the mineralization of H-type ferritins. The subsequent decay of these multiple Fe3+-oxy species to the superparamagnetic mineral suggests that Fe3+ species in different environments may be translocated as intact units from the protein shell into the ferritin cavity where the conversion to a solid mineral occurs.

1996
A.G., B, English MJ.  1996.  A Method for the Ventricular Late Potentials Detection and Characterisation using Wavelets. IEEE Engineering in Medicine and Biology Society. Abstract

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