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PubMed2005

Spectral characterization of two bioaccumulated methoxylated polybrominated diphenyl ethers.

Two methoxylated polybrominated diphenyl ethers (MeO-PBDEs) were isolated from a True's beaked whale (Mesoplodon mirus) and identified by NMR (1H, 1H-1H and 1H-13C) and high resolution mass spectrometry as 2-(2',4'-dibromophenoxy)-3,5-dibromoanisole (6-MeO-BDE47) and 2-(2',4'-dibromophenoxy)-4,6-dibromoanisole (2'-MeO-BDE68). Previously the structures of these bioaccumulated compounds have been determined by comparison of their mass spectra and gas chromatographic (GC) retention times with those of authentic standards. While this method is accepted and generally successful, NMR of the isolated compounds allows us to definitively identify the congeners. Our characterizations are consistent with those made for MeO-PBDEs in other organisms, identified by chromatographic methods.

Adipose Tissue↗
PubMed2005

Fibrillogenesis of apomyoglobin facilitated by aggregation sequence of yeast Sup35 in various regions.

To examine the effect of aggregation sequence QGGYQQQYNP from yeast Sup35 on fibril formation of sperm whale apomyoglobin (apoMb), we constructed several mutants via substitution. Urea-induced unfolding of apoMb confirms that the substitution of the aggregation sequence does not significantly affect the stability of the mutants compared to wild type (WT) at pH 4.2. Under this condition, however, despite the difference in rate most apoMb mutants form fibrils more readily than WT with distinct morphology. These results suggest that the aggregation sequence facilitates fibril assembly of apoMb at acidic pH in vitro and this facilitation depends on the regions replaced.

Amino Acid Sequence↗
PubMed2005

Atrioventricular conduction in mammalian species: hemodynamic and electrical scaling.

OBJECTIVES: The purpose of this study was to investigate scaling of the duration of late diastolic left ventricular (LV) filling in relation to AV conduction time (delay) (PR interval on the ECG) in mammals. BACKGROUND: From mouse to whale, AV delay increases 10-fold, whereas body mass increases one million-fold. The apparent "mismatch" results from scaling of AV delay versus body and heart mass. METHODS: We measured (1) mitral orifice diameter in 138 postmortem hearts of 48 mammalian species weighing between 17 g and 250 kg and (2) transmitral diastolic flow using magnetic resonance imaging (MRI) recordings of 10 healthy human individuals. (3) We visually inspected early and late diastolic LV filling. (4) We developed two physical models to explain scaling of late diastolic LV filling time. RESULTS: (1) Diameter of the mitral orifice proportionally relates to heart length (third root of heart mass). (2) Atrial contraction starts at a fixed instant (+/- 80%) of the (normalized) cardiac cycle and contributes 31% +/- 5% to LV filling. (3) MRI shows that during diastole, the left atrium (LA) and LV form a single space. (4) The physical models relate the duration of late diastolic LV filling directly to heart length, the third root of heart mass. CONCLUSIONS: (1) Late diastolic (LV) filling time scales with heart length (third root of heart mass). (2) No "mismatch" exists between AV delay and heart size. (3) Knowledge of the actual starting time of atrial contraction may contribute to better treatment of patients with heart failure. (4) The findings suggest that in evolution of mammalian species, hemodynamics commands electrical behavior of the heart.

Animals↗
PubMed2004

The effect of protein internal cavities on ligand migration and binding in myoglobin.

Using Fourier Transform Infrared Spectroscopy at cryogenic temperatures, we have studied carbon monoxide (CO) migration in the interior of sperm whale myoglobin and binding to teh heme iron. The effect of protein internal cavities was examined by comparing the wild-type protein with mutants in which the cavities were blocked by bulky amino acid sidechains. After photodissociation at 3 K, CO ligands reside in the primary docking site (B) from where they can migrate to other sites (C, D) that were identified as the Xe4 and Xe1 cavities. These studies were complemented by flash photolysis experiments at room temperature, which revealed that the protein cavities enable efficient excape of ligands from the protein after dissociation from the heme iron.

Animals↗
PubMed2004

Chlorobenzenes, chlorinated pesticides, coplanar chlorobiphenyls and other organochlorine compounds in Greenland biota.

This paper summarises the levels and composition of chlorobenzenes, chlorinated pesticides, coplanar polychlorinated biphenyls (PCBs) and the chlorinated compounds octachlorostyrene (OCS), hexachlorocyclobutadiene (HCBD) and pentachloro-anisole (PCA) in biota from the terrestrial, freshwater and marine environment of Greenland. The data were obtained during the second phase of the Arctic Monitoring and Assessment Programme (AMAP). Of the chlorobenzenes, hexachlorobenzene was the main constituent detected in almost all samples. The chlorobenzenes accumulate in the marine food web in a similar manner to the better-studied persistent organic pollutants, with maximum concentrations in beluga, minke whale and narwhal. However, concentrations in ringed seals and kittiwakes were lower than in marine fish, contradicting biomagnification. Of the organochlorine pesticides, the drin pesticides (aldrin, endrin, dieldrin) and heptachlor had increasing concentrations along the food chain, whilst biomagnification was less pronounced for endosulfan, methoxychlor and mirex. Endosulfan and methoxychlor are pesticides still in use and considered less persistent than other organochlorine pesticides. Their occurrence in Arctic biota is of particular concern, also given the high acute toxicity of endosulfan to fish. Chlorobenzene and pesticide concentrations tended to be lower in the Greenland samples than in the same animals from the Canadian Arctic, whilst their concentrations were similar to samples from Svalbard and Iceland. However, temporal trends might overlap the geographical differences. Coplanar chlorobiphenyls (CBs) were found in all samples analysed, with the maximum concentrations found in marine mammals such as beluga and narwhal. Biota from the terrestrial environment appeared to be less contaminated. The main contributor on a TEQ basis was CB126. OCS, HCBD and PCA were detected in biota from Greenland, although at very low concentrations. OCS seems to have the widest occurrence and the highest potential for biomagnification of the three compounds analysed.

Animals↗
PubMed2004

Dietary composition in Greenland 2000, plasma fatty acids and persistent organic pollutants.

UNLABELLED: Human exposure to pollution in the Arctic presents a potential future health risk for the local populations. Epidemiological studies in Greenland have shown that human blood levels of several organic contaminants are very high, especially in the North where people depend on local food. In East Greenland (Ittoqqortoormiit (Scoresbysund)) the population shows the highest blood levels of several persistent organic pollutants found in Arctic countries, especially PCB, the levels of which exceed Canadian guideline levels. As in other Arctic countries, the direct source of these contaminants is the diet, and it is, therefore important to monitor the composition of the diet along with other factors which may influence the metabolism and thereby the accumulation of toxic substances. This project is part of the human health program of the ongoing circumpolar 'Arctic Monitoring and Assessment Programme'. Dietary survey results (Semiquantitative Food Frequency questionnaire from 192 men and women from East Greenland and 48 men from Uummannaq West Greenland) were analysed along with other factors (lifestyle and anthropometric factors), blood lipids, fatty acid profiles, and concentrations of persistent organic pollutants (POPs). The dietary survey showed that the contributions of traditional food provided 25-30% of the total energy intake. However, the relative monthly meal intake of seal, whale, polar bear, fish and game, and the composition of imported food, varied between districts. The blood fatty acids (FA), e.g. the n-3/n-6 ratio (Uummannaq 0.70, Ittoqqortoormiit 0.37 Tassiilaq 0.45) showed moderate associations with the overall reported food composition. The n-3 fatty acids were associated with the well-known lowering effect on serum-triglyceride levels. The strongest associations between diet and plasma fatty acids were found for docosapentaenoic acid, C: 22.5.3 which strongly correlated with reported seal, and polar bear intake (P=0.01** and 0.04*, respectively), consistent with the fact that seal and polar bear blubber contain much higher concentrations of C: 22.5.3 than other sea mammals and fish. Seal and polar bear intake, and in particular all the plasma n-3 fatty acids, were significantly correlated with organic contaminant concentrations, (betaHCH, chlordanes, DDTs, Hexachlorobenzene, Mirex, PCBs, and toxaphenes) P<0.01**. CONCLUSIONS: The strongest correlations between POPs and fatty acids were found with C: 22.5.3, strongly indicating seal and polar bear blubber as the main contributors of POPs to the local population.

Adolescent↗
PubMed2004

Selenium status in Greenland Inuit.

In Greenland, the human intake of selenium has always been relatively high and is closely connected to intake of the traditional food of marine origin. Analyses of historic and present day human and animal hair samples have indicated that the selenium level in the marine environment has been constant over time, while the levels in humans have declined corresponding to a decrease in intake of traditional food. The Inuit population in Greenland is in dietary transition where western-style food will increasingly dominate. As a consequence, the ample supply of selenium may not be sustained in the future. We report here the selenium status in three Greenlandic population groups, Ittoqqortoormiit and Tasiilaq on the east coast and Uummannaq on the west coast. Mean whole blood concentrations ranged from 178 microg/l in Tasiilaq men to 488 microg/l in Uummannaq men. Plasma concentrations ranged from 79 microg/l in Tasiilaq women to 113 microg/l in Uummannaq men. With increasing Se concentrations in whole blood, the plasma concentrations increased but tended to stabilise a level approximately 140 microg/l. Selenium blood levels were highly significantly correlated with long chain marine fatty acids. Dietary survey and food composition data from the west coast showed that whale skin, muktuk, is the main source of Se followed by birds, seal meat and organs, and fish. Terrestrial animals contributed only insignificantly to the selenium intake. In West Greenland, daily Se intake (235 microg/day) was estimated by dietary survey; it corresponded well with a calculated intake (220 microg/day) based on the mean blood concentration.

Adolescent↗
PubMed2005

Spatial trends and factors affecting variation of organochlorine contaminants levels in Canadian Arctic beluga (Delphinapterus leucas).

Organochlorine pesticides and PCBs were analysed in blubber from beluga (Delphinapterus leucas), or white whales, collected at 15 sites in the Canadian Arctic between 1993 and 2001. The objective of the study was to define and interpret the spatial trends of major organic contaminants in northern beluga in terms of sources and transport pathways, and the biological factors influencing accumulation. When compared on a lipid weight basis, the concentrations of beta-HCH, cis-CHL and SigmaCHL, cis-nonachlor, heptachlor epoxide and p,p'-DDT were significantly higher in males than females at all five sites in the eastern Arctic where the two sexes were harvested. The differences were attributed to losses from the females during fetal development and lactation as reported in previous studies. Major compounds increased with age in males at most sites, however the lack of a significant increase with age at some sites was in part due to high organochlorine concentrations in young year classes (2-5 years), particularly at eastern sites such as Iqaluit and Pangnirtung. Lower concentrations of SigmaHCH and SigmaDDT compounds in young males in 2001 relative to 1995 at Hendrickson Island could be due to declining levels in the environment, changes in the diet, or differences in organochlorine loads transferred from the female after birth. Age-corrected least square mean concentrations in males showed significantly higher levels of many compounds, such as p,p'-DDE and SigmaCHB, at south Baffin Island sites than those in the west. Two notable exceptions were HCBz and beta-HCH which were higher in the west. Methoxyclor was detected in males at Sanikiluaq (58 ng g-1) and in both sexes at Kimmirut, but at no other sites. Principal component analysis grouped the 16 sites into five major groupings based on the similarity of normalised organochlorine pesticide and PCB levels. Sites from the western Arctic were grouped by higher proportions of HCBz, beta-HCH and gamma-HCH and higher chlorinated PCBs. Endosulfan and alpha-HCH comprised a larger proportion of total organochlorine residues in the northern Hudson Bay sites, while methoxychlor, chlordane compounds and octachlorobiphenyls were enriched at Sanikiluaq in eastern Hudson Bay. The analysis showed that the relative amounts of several key compounds are similar in the beluga stocks over large spatial areas (i.e. eastern versus western sites), however, some stocks have distinct fingerprints which can be used to differentiate them from adjacent stocks. Ratios of major HCH isomers largely corresponded with air and surface water measurements conducted during the 1990s, but low alpha-/beta- and alpha-/gamma-HCH ratios in all three western Arctic collections indicate rapid losses of the alpha-isomer from the food web, proportionately higher beta- and gamma-isomers in the Beaufort Sea, or a combination of the two processes. Chlordane residue patterns generally correspond to those from previous studies, however, interpretation of spatial trends are difficult due to the aging of the probable sources in the south, possible atmospheric input from new sources and complex transport pathways.

Adipose Tissue↗
PubMed1991

Coordination structure and chemical reactivity of hemoprotein-butyl peroxide complex.

ESR and optical spectra ascribed to be the hemoprotein-butylperoxide complex were detected for the frozen aqueous solution containing whale met-Mb and t- or n-butylhydroperoxide at pH 10. The observed ESR and optical parameters of the complex were characteristic to those of six coordinate ferric low-spin complexes, having the butylperoxide anion at the axial position of heme. pH dependent ESR measurements demonstrated the formation of the complex in the biological pH regions (7.0). Time dependent ESR and optical measurements indicated that the complex may be one of the intermediate species in the processes of heme degradation reaction induced by butylperoxide.

Animals↗
PubMed1989

Proton NMR study of the influence on iron oxidation/ligation/spin state on the heme orientational preference in myoglobin.

Proton nuclear magnetic resonance spectroscopy has been utilized to demonstrate that the degree of heme orientational disorder within a given myoglobin protein matrix can be a sensitive function of the oxidation/ligation/spin state of the heme iron. For sperm whale deuterohemin-reconstituted myoglobin, the equilibrium was found to strongly favor (5.7 to 7.8 kJ/mol) the X-ray characterized heme orientation in all six-coordinate states, but with a considerable reduction in preference (to 1.6 kJ/mol) in the five-coordinate deoxy state. In native yellow fin tuna myoglobin, changes in heme orientational preferences of approximately 3 kJ/mol occur even between two six-coordinate ferric states differing solely in spin states.

Animals↗
PubMed2000

Salt effects on ionization equilibria of histidines in myoglobin.

The salt dependence of histidine pK(a) values in sperm whale and horse myoglobin and in histidine-containing peptides was measured by (1)H-NMR spectroscopy. Structure-based pK(a) calculations were performed with continuum methods to test their ability to capture the effects of solution conditions on pK(a) values. The measured pK(a) of most histidines, whether in the protein or in model compounds, increased by 0.3 pH units or more between 0.02 M and 1.5 M NaCl. In myoglobin two histidines (His(48) and His(36)) exhibited a shallower dependence than the average, and one (His(113)) showed a steeper dependence. The (1)H-NMR data suggested that the salt dependence of histidine pK(a) values in the protein was determined primarily by the preferential stabilization of the charged form of histidine with increasing salt concentrations rather than by screening of electrostatic interactions. The magnitude and salt dependence of interactions between ionizable groups were exaggerated in pK(a) calculations with the finite-difference Poisson-Boltzmann method applied to a static structure, even when the protein interior was treated with arbitrarily high dielectric constants. Improvements in continuum methods for calculating salt effects on pK(a) values will require explicit consideration of the salt dependence of model compound pK(a) values used for reference in the calculations.

Animals↗
PubMed2001

The Fe(2+)-His(F8) Raman band shape of deoxymyoglobin reveals taxonomic conformational substates of the proximal linkage.

The band shape of the Raman line attributed to the Fe(2+)-N(epsilon)(His(F8)) stretching mode in deoxymyoglobin contains significant information on the nature of the Fe-His proximal linkage. Raman lines appearing close to it, however, obscure the true line profile. To isolate this from its accompanying lines we use its isotopic shift of approximately 1 cm(-1) when (56)Fe in natural-abundance deoxymyoglobin is substituted by (54)Fe. This enables us to isolate the true line shape. We have measured this line shape in sperm whale myoglobin dissolved in a 66% vol/vol glycerol/water solution for nine temperatures from 10 K to 300 K. The nu(Fe-His) band shows a complex temperature-dependent profile, with a shoulder on its high-frequency wing, which becomes more prominent with increasing temperature. Detailed analysis reveals that the band is composed of five distinct lines attributable to taxonomic conformational substates of the nu(Fe-His) linkage. These are in thermodynamic equilibrium above the glass transition temperature T(f) but freeze in into the thermodynamic distribution at T(f) for lower temperatures. Alternative models that try to explain the nu(Fe-His) band shape by either an anharmonic coupling of the nu(Fe-His) to a low-frequency heme doming mode or by conformational substates related to a Gaussian distribution of iron out-of-plane displacements are at variance with the distinct features observed experimentally.

Animals↗
PubMed1980

Structural dynamics of liganded myoglobin.

X-ray crystallography can reveal the magnitudes and principal directions of the mean-square displacements of every atom in a protein. This structural information is complementary to the temporal information obtainable by spectroscopic techniques such as nuclear magnetic resonance. Determination of the temperature dependence of the mean-square displacements makes it possible to separate large conformational motions from simple thermal vibrations. The contribution of crystal lattice disorder to the overall apparent displacement can be estimated by Mössbauer spectroscopy. This technique has been applied to high resolution x-ray diffraction data from sperm whale myoglobin in its Met iron and oxy cobalt forms. Both crystal structures display regions of large conformational motions, particularly at the chain termini and in the region of the proximal histidine. Overall, the mean-square displacement increases with increasing distance from the center of gravity of the molecule. Some regions of the heme pocket in oxy cobalt myoglobin are more rigid than the corresponding regions in Met myoglobin.

Animals↗
PubMed1981

Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole.

The assigned exchangeable proton signals in the proton nuclear magnetic resonance spectra of sperm whale deoxy and Met-cyano myoglobin in H2O solution were found to exhibit pH-dependent saturation transfer from the bulk water, which allowed determination of the kinetics and mechanism of the labile proton exchange with solvent. The exchange rates are base catalyzed for both protein forms, with the rate eight times faster in Met-cyano than in deoxy myoglobin. The exchange rate is taken as a measure of the magnitude of the fluctuation in the protein conformation near the heme cavity. On the basis of tritium exchange methods, the greater stability of the unligated relative to the ligated state in myoglobin has also been reported for hemoglobin. The present study, however, localizes the differential kinetic stability on the F helix whose flexibility has been implicated in the mechanism of cooperativity. The observation that filling the hydrophobic vacancy on the proximal side of the heme near the proximal histidine in Met-cyano myoglobin wih cyclopropane increases the proton lability argues against the role for this hole in facilitating the flexibility of the F helix in the native protein.

Animals↗
PubMed1983

Proton magnetic resonance study of the influence of heme 2,4 substituents on the exchange rates of labile protons in the heme pocket of myoglobin.

Four exchangeable protons with large hyperfine shifts are assigned in the heme pocket of sperm whale met-cyano myoglobin reconstituted with heme possessing acetyl groups, ethyl groups, bromines, and hydrogens at the 2,4 position, using both relaxation and chemical-shift data. The four protons arise from the ring NH's of the proximal (F8), distal (E7), and FG2 histidines, and the peptide NH of His F8. The similarity of all chemical shifts to those of the native protein as well as the invariance of the relaxation rates of the distal histidyl ring NH dictate essentially the same structure for the heme cavity of both native and reconstituted proteins. The exchange rates with bulk water of the four labile proteins in each modified protein were determined by saturation-transfer and line width methods. All four labile protons were found to have the same exchange rate as in the native protein for acetyl and ethyl 2,4 substituents; the two resolved labile protons in the derivative with 2,4 bromine were also unchanged. The reconstituted protein with hydrogens at the 2,4 position exhibited slower exchange rates for three of the four protons, indicating an increased dynamic stability of the heme pocket in the absence of bulky 2,4 substituents.

Animals↗
PubMed1983

Resonance Raman studies of Co-O2 and O-O stretching vibrations in oxy-cobalt hemes.

Strong evidence suggests that the stretching vibration of the bound oxygen can be perturbed by an accidentally degenerate porphyrin ring mode, resulting in two split frequencies. In the Co(II)(TpivPP) (pyridine) (18)O(2) complex, we demonstrate that the nu((18)O-(18)O) mode, after being shifted from its nu((16)O-(16)O) value at 1,156 cm(-1), undergoes a resonance interaction with the 1,080 cm(-1) porphyrin mode, giving rise to two lines at 1,067 and 1,089 cm(-1). In the O(2) complex of Co(II) mesoporphyrin IX-substituted sperm whale myoglobin, we observed a dramatic intensity increase at 1,132 cm(-1) upon (16)O(2) --> (18)O(2) substitution, which is due to the reappearance of the 1,132-cm(-1) porphyrin mode after the removal of resonance conditions. A decrease in O(2) binding affinity, caused by the proximal base tension, corresponds to an increase in the Co-O(2) stretching frequency. The nu(Co-O(2)) at 527 cm(-1) for the low affinity Co(II)(TpivPP)(1,2-Me(2)Im) O(2) complex is 11 cm(-1) higher than the 516-cm(-1) value for the high affinity complex (with N-MeIm replacing 1,2-Me(2)Im). However, in the corresponding iron complexes the reverse behavior is observed, i.e., the nu(Fe-O(2)) decreases for the (1,2-Me(2)Im) complex. There is a 24-cm(-1) difference in the Co-O(2) stretching frequencies between Co(II)(TpivPP)(N-MeIm)O(2) (at 516 cm(-1)) and oxy meso CoMb (at 540 cm(-1)), suggesting a protein induced distortion of the Co-O-O linkage. However, the values for nu(Fe-O(2)) are nearly identical between Fe(II)(TpivPP)(N-MeIm)O(2) (at 571 cm(-1)) and oxy Mb (at 573 cm(-1)), indicating that O(2) binds to myoglobin in the same manner as in the sterically unhindered "picket fence" complex. Evidence is presented that suggests the presence of two dioxygen stretching frequencies due to two different conformers in each of the N-MeIm and 1,2-Me(2)Im complex of oxy Co(II)(TpivPP).

Animals↗
PubMed1987

Fluorescence and energy transfer of tryptophans in Aplysia myoglobin.

The fluorescence decay of tryptophan residues in apo and met Aplysia limacina myoglobin and sperm whale myoglobin were measured in aqueous solution at 10 degrees-15 degrees C. In all species, multiexponential behavior was observed in which the individual components displayed unique frequency-dependent emission characteristics. The results suggest that the tryptophan fluorescence in all met samples are quenched by rapid Forster energy transfer to the heme as predicted from the crystal geometry. Fluorescence from the apo protein is similar to that in solutions of free tryptophans. In addition, the fluorescence properties of the reversible thermal denaturation of Aplysia limacina met myoglobin was investigated between 25 degrees and 75 degrees C.

Animals↗
PubMed1988

Adsorption of the protein antigen myoglobin affects the binding of conformation-specific monoclonal antibodies.

Five monoclonal antibodies against sperm whale myoglobin have been used to investigate the physical state of the antigen adsorbed onto a polydimethylsiloxane surface. The binding of each antibody is sensitive to the antigen's conformation in solution while the locations of the antigenic sites on the myoglobin molecule for three of the antibodies have been determined (Berzofsky, J.A., G.K. Buckenmeyer, G. Hicks, F.R.N. Gurd, R.J. Feldmann, and J. Minna. 1982. J. Biol. Chem. 257:3189-3198). The binding of the fluorescein isothiocyanate-labeled IgG and Fab antibodies to previously adsorbed myoglobin has been observed using total internal reflection fluorescence. Three of the antibodies bind specifically to surface-adsorbed myoglobin with affinities at least 50% relative to myoglobin in solution whereas two of the antibodies show affinities for the surface-adsorbed myoglobin diminished by at least two orders of magnitude relative to myoglobin in solution. The specific loss of certain antigenic determinants on the adsorbed myoglobin, coupled with the retention of others, indicates a nonrandom adsorption of the myoglobin molecules.

Adsorption↗

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