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  • 1
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    Moonlight enhances growth in larval fish (2019)
    Wiley
    In: Ecology
    Details
    Publication Date: 2019
    Description: Abstract Moonlight mediates trophic interactions and shapes the evolution of life‐history strategies for nocturnal organisms. Reproductive cycles and important life‐history transitions for many marine organisms coincide with moon phases, but few studies consider the effects of moonlight on pelagic larvae at sea. We evaluated effects of moonlight on growth of pelagic larvae of a temperate reef fish using “master chronologies” of larval growth constructed from age‐independent daily increment widths recorded in otoliths of 321 individuals. We found that daily growth rates of fish larvae were enhanced by lunar illumination after controlling for the positive influence of temperature and the negative influence of cloud cover. Collectively, these results indicate that moonlight enhances growth rates of larval fish. This pattern is likely the result of moonlight's combined effects on foraging efficiency and suppression of diel migrations of mesopelagic predators, and has the potential to drive evolution of marine life histories.
    Print ISSN: 0012-9658
    Electronic ISSN: 1939-9170
    Topics: Biology
    Published by Wiley on behalf of The Ecological Society of America (ESA).
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  • 2
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    Evidence and population consequences of shared larval dispersal histories in a marine fish (2016)
    Wiley
    In: Ecology
    Details
    Publication Date: 2016-01-30
    Description: Larval dispersal is disproportionately important for marine population ecolgy and evolution, yet our inability to track individuals severely constrains our understanding of this key process. We analyze otoliths of a small reef fish, the common triplefin ( Forsterygion lapillum ), to reconstruct individual dispersal histories and address the following questions: (1) How many discrete sets of dispersal histories (dispersal cohorts) contribute to replenishment of focal populations; (2) When do dispersal cohorts converge (a metric of shared dispersal histories among cohorts); and (3) Do these patterns predict spatiotemporal variation in larval supply? We used light traps to quantify larval supply, and otolith microstructure and microchemistry (using laser ablation inductively coupled plasma mass spectrometry; LA-ICP-MS) to reconstruct daily environmental histories of individuals in their 30-d lead-up to settlement. Our results indicate that a variable number of dispersal cohorts replenish focal populations (range of 2–8, mean of 4.3, standard deviation of 2.8). Convergence times varied (from 0 to 〉30 d prior to settlement), and larval supply was negatively correlated with cohort evenness but not with the number of cohorts, or when they converged, indicating disproportionately large contributions from some cohorts (i.e., sweepstakes events). Collectively, our results suggest that larval reef fishes may variably disperse in shoals, to drive local replenishment and connectivity within a metapopulation.
    Print ISSN: 0012-9658
    Electronic ISSN: 1939-9170
    Topics: Biology
    Published by Wiley on behalf of The Ecological Society of America (ESA).
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  • 3
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    Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Methyl-coenzyme M reductase (MCR), the enzyme responsible for the microbial formation of methane, is a 300-kilodalton protein organized as a hexamer in an alpha2beta2gamma2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum, determined at 1.45 angstrom resolution for the inactive enzyme state MCRox1-silent, reveals that two molecules of the nickel porphinoid coenzyme F430 are embedded between the subunits alpha, alpha', beta, and gamma and alpha', alpha, beta', and gamma', forming two identical active sites. Each site is accessible for the substrate methyl-coenzyme M through a narrow channel locked after binding of the second substrate coenzyme B. Together with a second structurally characterized enzyme state (MCRsilent) containing the heterodisulfide of coenzymes M and B, a reaction mechanism is proposed that uses a radical intermediate and a nickel organic compound.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ermler, U -- Grabarse, W -- Shima, S -- Goubeaud, M -- Thauer, R K -- New York, N.Y. -- Science. 1997 Nov 21;278(5342):1457-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biophysik, Heinrich-Hoffmann-Strabetae 7, 60528 Frankfurt, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9367957" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Coenzymes/chemistry/metabolism ; Crystallography, X-Ray ; Disulfides/chemistry/metabolism ; Hydrogen/metabolism ; Hydrogen Bonding ; Ligands ; Mesna/analogs & derivatives/chemistry/metabolism ; Metalloporphyrins/chemistry/metabolism ; Methane/*metabolism ; Methanobacterium/*enzymology ; Models, Molecular ; Nickel/chemistry/metabolism ; Oxidation-Reduction ; Oxidoreductases/*chemistry/*metabolism ; Phosphothreonine/analogs & derivatives/chemistry/metabolism ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Interactive effects of shelter and conspecific density shape mortality, growth, and condition in juvenile reef fish (2016)
    Wiley
    In: Ecology
    Details
    Publication Date: 2016-04-12
    Description: How landscape context influences density-dependent processes is important, as environmental heterogeneity can confound estimates of density dependence in demographic parameters. Here we evaluate 19 populations in a shoaling temperate reef fish ( Trachinops caudimaculatus ) metapopulation within a heterogeneous seascape (Port Phillip Bay, Australia) to show empirically that shelter availability and population density interact to influence juvenile mortality, growth and condition. Although heterogeneity in shelter availability obscured the underlying patterns of density dependence in different ways, the combination of habitat and its interaction with density were two to six times more important than density alone in explaining variation in demographic parameters for juveniles. These findings contradict many small-scale studies and highlight the need for landscape-scale observations of how density dependence interacts with resource availability and competition to better understand how demographic parameters influence the dynamics of metapopulations in heterogeneous environments. This article is protected by copyright. All rights reserved.
    Print ISSN: 0012-9658
    Electronic ISSN: 1939-9170
    Topics: Biology
    Published by Wiley on behalf of The Ecological Society of America (ESA).
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  • 5
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    Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-11-29
    Description: The anaerobic oxidation of methane (AOM) with sulphate, an area currently generating great interest in microbiology, is accomplished by consortia of methanotrophic archaea (ANME) and sulphate-reducing bacteria. The enzyme activating methane in methanotrophic archaea has tentatively been identified as a homologue of methyl-coenzyme M reductase (MCR) that catalyses the methane-forming step in methanogenic archaea. Here we report an X-ray structure of the 280 kDa heterohexameric ANME-1 MCR complex. It was crystallized uniquely from a protein ensemble purified from consortia of microorganisms collected with a submersible from a Black Sea mat catalysing AOM with sulphate. Crystals grown from the heterogeneous sample diffract to 2.1 A resolution and consist of a single ANME-1 MCR population, demonstrating the strong selective power of crystallization. The structure revealed ANME-1 MCR in complex with coenzyme M and coenzyme B, indicating the same substrates for MCR from methanotrophic and methanogenic archaea. Differences between the highly similar structures of ANME-1 MCR and methanogenic MCR include a F(430) modification, a cysteine-rich patch and an altered post-translational amino acid modification pattern, which may tune the enzymes for their functions in different biological contexts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shima, Seigo -- Krueger, Martin -- Weinert, Tobias -- Demmer, Ulrike -- Kahnt, Jorg -- Thauer, Rudolf K -- Ermler, Ulrich -- England -- Nature. 2011 Nov 27;481(7379):98-101. doi: 10.1038/nature10663.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Terrestrial Microbiology, Karl-Frisch-Strasse 10, D-35043 Marburg, Germany. shima@mpi-marburg.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22121022" target="_blank"〉PubMed〈/a〉
    Keywords: Anaerobiosis ; Archaea/*enzymology/isolation & purification/metabolism ; *Biocatalysis ; Black Sea ; Catalytic Domain ; Coenzymes/chemistry/metabolism ; Crystallography, X-Ray ; Cysteine/metabolism ; Expeditions ; Methane/*metabolism ; Models, Molecular ; Oxidation-Reduction ; Oxidoreductases/*chemistry/*metabolism ; Protein Conformation ; Seawater/*microbiology ; Ships ; Sulfates/metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 6
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    The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-07-26
    Description: Biological formation and consumption of molecular hydrogen (H2) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp2-hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar to those of cyanide. The three-dimensional arrangement of the ligands is similar to that of thiolate, CO, and cyanide ligated to the low-spin iron in binuclear [NiFe]- and [FeFe]-hydrogenases, although the enzymes have evolved independently and the CO and cyanide ligands are not found in any other metalloenzyme. The related iron ligation pattern of hydrogenases exemplifies convergent evolution and presumably plays an essential role in H2 activation. This finding may stimulate the ongoing synthesis of catalysts that could substitute for platinum in applications such as fuel cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shima, Seigo -- Pilak, Oliver -- Vogt, Sonja -- Schick, Michael -- Stagni, Marco S -- Meyer-Klaucke, Wolfram -- Warkentin, Eberhard -- Thauer, Rudolf K -- Ermler, Ulrich -- New York, N.Y. -- Science. 2008 Jul 25;321(5888):572-5. doi: 10.1126/science.1158978.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Terrestrische Mikrobiologie and Laboratorium fur Mikrobiologie, Fachbereich Biologie, Philipps-Universitat Marburg, Karl-von-Frisch-Strasse, D-35043 Marburg, Germany. shima@mpi-marburg.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18653896" target="_blank"〉PubMed〈/a〉
    Keywords: Apoenzymes/chemistry ; Binding Sites ; Carbon Monoxide/chemistry ; Catalytic Domain ; Coenzymes/chemistry ; Crystallography, X-Ray ; Cyanides/chemistry/metabolism ; Dimerization ; Evolution, Molecular ; Holoenzymes/chemistry ; Hydrogen/chemistry/*metabolism ; Hydrogenase/*chemistry/isolation & purification/metabolism ; Iron/chemistry ; Ligands ; Methane/biosynthesis ; Methanococcales/*enzymology ; Models, Molecular ; Oxidation-Reduction ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 7
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    Born at the right time? A conceptual framework linking reproduction, development, and settlement in reef fish (2017)
    Wiley
    In: Ecology
    Details
    Publication Date: 2017-10-16
    Description: Parents are expected to make decisions about reproductive timing and investment that maximize their own fitness, even if this does not maximize the fitness of each individual offspring. When offspring survival is uncertain, selection typically favors iteroparity, which means that offspring born at some times can be disadvantaged, while others get lucky. The eventual fate of offspring may be further modified by their own decisions. Are fates of offspring set by birthdates (i.e., determined by parents), or can offspring improve upon the cards they've been dealt? If so, do we see adaptive plasticity in the developmental timing of offspring? We evaluate these questions for a coral reef fish (the sixbar wrasse, Thalassoma hardwicke ) that is characterized by extreme iteroparity and flexible larval development. Specifically, we monitored larval settlement to 192 small reefs over 11 lunar months and found that most fish settled during new moons of a lunar cycle (consistent with preferential settlement on dark nights). Settlement was significantly lower than expected by chance during the full moon and last quarter of the lunar cycle (consistent with avoidance of bright nights). Survival after settlement was greatest for fish that settled during times of decreasing lunar illumination (from last quarter to new moon). Fish that settled on the last quarter of the lunar cycle were ~10% larger than fish that settled during other periods, suggesting larvae delay settlement to avoid the full moon. These results are consistent with a numerical model that predicts plasticity in larval development time that enables avoidance of settlement during bright periods. Collectively, our results suggest that fish with inauspicious birthdates may alter their developmental trajectories to settle at better times. We speculate that such interactions between parent and offspring strategies may reinforce the evolution of extreme iteroparity and drive population dynamics, by increasing the survival of offspring born at the “wrong” time by allowing them to avoid the riskiest times of settlement. This article is protected by copyright. All rights reserved.
    Print ISSN: 0012-9658
    Electronic ISSN: 1939-9170
    Topics: Biology
    Published by Wiley on behalf of The Ecological Society of America (ESA).
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  • 8
    Electronic Resource
    Electronic Resource
    Effects of the metals, Be, Fe, Cu and Al, on the mobility of immunoglobulin receptors (1982)
    Springer
    Cellular and molecular life sciences 38 (1982), S. 1227-1228 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Cap formation in mouse spleen cells induced by antiimmunoglobulin was inhibited by the metals Be, Fe, Cu and Al. Be was especially strong as an inhibitor of cap formation. It is suggested that these metals might change the mobility of the membrane and have some biological effects on the cross association of antigen receptors when B lymphocytes are attached by them.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01959755
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  • 9
    Electronic Resource
    Electronic Resource
    A study of the effect of the fabrication process on diffusion in a layered thin film (1999)
    Springer
    Microsystem technologies 5 (1999), S. 169-172 
    Details
    ISSN: 1432-1858
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Technology
    Notes: Abstract  A diffusion layer that is likely to be formed at the interfaces of the multi-layered thin film would affect its overall mechanical properties; the thinner the thin film, the more significant would be the effect. We measure the distribution of atoms and estimate the thickness of the diffusion layer at the vicinity of the interfaces among thin films of Al and SiO2 and silicon wafer with the aid of Auger electron spectroscopy (AES). The effect of heat treatment after fabrication of the thin films on the diffusion is also investigated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s005420050159
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  • 10
    Electronic Resource
    Electronic Resource
    Purification, characterization, and primary structure of a monofunctional catalase from Methanosarcina barkeri (1999)
    Springer
    Archives of microbiology 171 (1999), S. 317-323 
    Details
    ISSN: 1432-072X
    Keywords: Key words Catalase ; Cytochromes ; Heme ; Methanosarcina ; Methanogenic archaea
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Methanosarcina barkeri is a strictly anaerobic, cytochrome-containing, methane-forming archaeon. We report here that the microorganism contains a catalase, which was purified and characterized. The enzyme with an apparent molecular mass of 190 kDa was shown to be composed of four identical subunits of apparent molecular mass of 54 kDa. The heme-containing enzyme did not exhibit peroxidase activity, which indicates that it is a monofunctional catalase. This is substantiated by the primary structure, which is related to that of other monofunctional catalases rather than to that of bifunctional catalase-peroxidases. The enzyme showed an [S]0.5V for H2O2 of 25 mM and an apparent V max of 200,000 U/mg; it was inhibited by azide ([I]0.5V = 1 μM) and cyanide ([I]0.5V = 5 μM) and inactivated by 1,2,4-aminotriazole. The activity was almost independent of the pH (between pH 4 and 10) and the temperature (between 15 °C and 55 °C). Comparison of the primary structure of monofunctional catalases revealed that the enzyme from M. barkeri is most closely related to the monofunctional catalase of Dictyostelium discoideum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050716
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