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  • 1
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-02-05
    Description: The sterile alpha motif (SAM) domain is a protein interaction module that is present in diverse signal-transducing proteins. SAM domains are known to form homo- and hetero-oligomers. The crystal structure of the SAM domain from an Eph receptor tyrosine kinase, EphB2, reveals two large interfaces. In one interface, adjacent monomers exchange amino-terminal peptides that insert into a hydrophobic groove on each neighbor. A second interface is composed of the carboxyl-terminal helix and a nearby loop. A possible oligomer, constructed from a combination of these binding modes, may provide a platform for the formation of larger protein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thanos, C D -- Goodwill, K E -- Bowie, J U -- New York, N.Y. -- Science. 1999 Feb 5;283(5403):833-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉UCLA-DOE Laboratory of Structural Biology and Molecular Medicine and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9933164" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; GRB10 Adaptor Protein ; Humans ; Hydrogen Bonding ; Kinesin/metabolism ; Models, Molecular ; Myosins/metabolism ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Receptor Aggregation ; Receptor Protein-Tyrosine Kinases/*chemistry/metabolism ; Receptor, EphB2 ; Recombinant Proteins/chemistry/metabolism ; Surface Properties
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2008-05-27
    Description: Understanding the energetics of molecular interactions is fundamental to all of the central quests of structural biology including structure prediction and design, mapping evolutionary pathways, learning how mutations cause disease, drug design, and relating structure to function. Hydrogen-bonding is widely regarded as an important force in a membrane environment because of the low dielectric constant of membranes and a lack of competition from water. Indeed, polar residue substitutions are the most common disease-causing mutations in membrane proteins. Because of limited structural information and technical challenges, however, there have been few quantitative tests of hydrogen-bond strength in the context of large membrane proteins. Here we show, by using a double-mutant cycle analysis, that the average contribution of eight interhelical side-chain hydrogen-bonding interactions throughout bacteriorhodopsin is only 0.6 kcal mol(-1). In agreement with these experiments, we find that 4% of polar atoms in the non-polar core regions of membrane proteins have no hydrogen-bond partner and the lengths of buried hydrogen bonds in soluble proteins and membrane protein transmembrane regions are statistically identical. Our results indicate that most hydrogen-bond interactions in membrane proteins are only modestly stabilizing. Weak hydrogen-bonding should be reflected in considerations of membrane protein folding, dynamics, design, evolution and function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2734483/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2734483/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joh, Nathan Hyunjoong -- Min, Andrew -- Faham, Salem -- Whitelegge, Julian P -- Yang, Duan -- Woods, Virgil L -- Bowie, James U -- R01 CA081000/CA/NCI NIH HHS/ -- R01 CA081000-07/CA/NCI NIH HHS/ -- R01 CA081000-08/CA/NCI NIH HHS/ -- R01 CA081000-09/CA/NCI NIH HHS/ -- R01 GM063919/GM/NIGMS NIH HHS/ -- R01 GM063919-06/GM/NIGMS NIH HHS/ -- R01 GM063919-07/GM/NIGMS NIH HHS/ -- R01 GM063919-08/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 Jun 26;453(7199):1266-70. doi: 10.1038/nature06977. Epub 2008 May 25.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18500332" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriorhodopsins/chemistry/genetics/metabolism ; Crystallography, X-Ray ; Deuterium Exchange Measurement ; Hydrogen Bonding ; Membrane Proteins/*chemistry/genetics/*metabolism ; Models, Molecular ; Mutation/genetics ; Protein Folding ; Solubility ; Thermodynamics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 3
    Publication Date: 1990-03-16
    Description: An amino acid sequence encodes a message that determines the shape and function of a protein. This message is highly degenerate in that many different sequences can code for proteins with essentially the same structure and activity. Comparison of different sequences with similar messages can reveal key features of the code and improve understanding of how a protein folds and how it performs its function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowie, J U -- Reidhaar-Olson, J F -- Lim, W A -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Mar 16;247(4948):1306-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2315699" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Computer Graphics ; *DNA-Binding Proteins ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Proteins/*physiology/ultrastructure ; Repressor Proteins ; Structure-Activity Relationship ; Surface Properties ; Viral Proteins ; Viral Regulatory and Accessory Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1991-07-12
    Description: The inverse protein folding problem, the problem of finding which amino acid sequences fold into a known three-dimensional (3D) structure, can be effectively attacked by finding sequences that are most compatible with the environments of the residues in the 3D structure. The environments are described by: (i) the area of the residue buried in the protein and inaccessible to solvent; (ii) the fraction of side-chain area that is covered by polar atoms (O and N); and (iii) the local secondary structure. Examples of this 3D profile method are presented for four families of proteins: the globins, cyclic AMP (adenosine 3',5'-monophosphate) receptor-like proteins, the periplasmic binding proteins, and the actins. This method is able to detect the structural similarity of the actins and 70- kilodalton heat shock proteins, even though these protein families share no detectable sequence similarity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowie, J U -- Luthy, R -- Eisenberg, D -- New York, N.Y. -- Science. 1991 Jul 12;253(5016):164-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024-1570.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1853201" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/chemistry/ultrastructure ; Algorithms ; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry ; *Escherichia coli Proteins ; Molecular Structure ; Myoglobin/chemistry/ultrastructure ; *Periplasmic Binding Proteins ; *Protein Conformation ; Proteins/*chemistry ; Receptors, Cyclic AMP/chemistry/ultrastructure ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2006-01-28
    Description: The postsynaptic density (PSD) is a complex assembly of proteins associated with the postsynaptic membrane that organizes neurotransmitter receptors, signaling pathways, and regulatory elements within a cytoskeletal matrix. Here we show that the sterile alpha motif domain of rat Shank3/ProSAP2, a master scaffolding protein located deep within the PSD, can form large sheets composed of helical fibers stacked side by side. Zn2+, which is found in high concentrations in the PSD, binds tightly to Shank3 and may regulate assembly. Sheets of the Shank protein could form a platform for the construction of the PSD complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baron, Marisa K -- Boeckers, Tobias M -- Vaida, Bianca -- Faham, Salem -- Gingery, Mari -- Sawaya, Michael R -- Salyer, Danielle -- Gundelfinger, Eckart D -- Bowie, James U -- R01 CA081000/CA/NCI NIH HHS/ -- R01 GM063919/GM/NIGMS NIH HHS/ -- R01 GM063919-07/GM/NIGMS NIH HHS/ -- R01 GM063919-08/GM/NIGMS NIH HHS/ -- R01 GM075922/GM/NIGMS NIH HHS/ -- R01 GM075922-04/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Jan 27;311(5760):531-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Molecular Biology Institute, University of California, Los Angeles, 611 Charles E. Young Drive East, Los Angeles, CA 90095-1570, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439662" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/analysis/*chemistry/genetics/metabolism ; Animals ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Hippocampus/chemistry ; Microscopy, Electron ; Models, Molecular ; Mutation ; Nerve Tissue Proteins ; Neurons/chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; Rats ; Recombinant Fusion Proteins/analysis ; Solubility ; Synapses/*chemistry ; Zinc/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 2008-06-28
    Description: Deep avian evolutionary relationships have been difficult to resolve as a result of a putative explosive radiation. Our study examined approximately 32 kilobases of aligned nuclear DNA sequences from 19 independent loci for 169 species, representing all major extant groups, and recovered a robust phylogeny from a genome-wide signal supported by multiple analytical methods. We documented well-supported, previously unrecognized interordinal relationships (such as a sister relationship between passerines and parrots) and corroborated previously contentious groupings (such as flamingos and grebes). Our conclusions challenge current classifications and alter our understanding of trait evolution; for example, some diurnal birds evolved from nocturnal ancestors. Our results provide a valuable resource for phylogenetic and comparative studies in birds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hackett, Shannon J -- Kimball, Rebecca T -- Reddy, Sushma -- Bowie, Rauri C K -- Braun, Edward L -- Braun, Michael J -- Chojnowski, Jena L -- Cox, W Andrew -- Han, Kin-Lan -- Harshman, John -- Huddleston, Christopher J -- Marks, Ben D -- Miglia, Kathleen J -- Moore, William S -- Sheldon, Frederick H -- Steadman, David W -- Witt, Christopher C -- Yuri, Tamaki -- New York, N.Y. -- Science. 2008 Jun 27;320(5884):1763-8. doi: 10.1126/science.1157704.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoology Department, Field Museum of Natural History, 1400 South Lake Shore Drive, Chicago, IL 60605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18583609" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Animals ; Biological Evolution ; Birds/*classification/*genetics ; Ecosystem ; Flight, Animal ; *Genome ; *Genomics ; Molecular Sequence Data ; *Phylogeny ; Sequence Alignment ; Sequence Analysis, DNA
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 2014-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rocha, L A -- Aleixo, A -- Allen, G -- Almeda, F -- Baldwin, C C -- Barclay, M V L -- Bates, J M -- Bauer, A M -- Benzoni, F -- Berns, C M -- Berumen, M L -- Blackburn, D C -- Blum, S -- Bolanos, F -- Bowie, R C K -- Britz, R -- Brown, R M -- Cadena, C D -- Carpenter, K -- Ceriaco, L M -- Chakrabarty, P -- Chaves, G -- Choat, J H -- Clements, K D -- Collette, B B -- Collins, A -- Coyne, J -- Cracraft, J -- Daniel, T -- de Carvalho, M R -- de Queiroz, K -- Di Dario, F -- Drewes, R -- Dumbacher, J P -- Engilis, A Jr -- Erdmann, M V -- Eschmeyer, W -- Feldman, C R -- Fisher, B L -- Fjeldsa, J -- Fritsch, P W -- Fuchs, J -- Getahun, A -- Gill, A -- Gomon, M -- Gosliner, T -- Graves, G R -- Griswold, C E -- Guralnick, R -- Hartel, K -- Helgen, K M -- Ho, H -- Iskandar, D T -- Iwamoto, T -- Jaafar, Z -- James, H F -- Johnson, D -- Kavanaugh, D -- Knowlton, N -- Lacey, E -- Larson, H K -- Last, P -- Leis, J M -- Lessios, H -- Liebherr, J -- Lowman, M -- Mahler, D L -- Mamonekene, V -- Matsuura, K -- Mayer, G C -- Mays, H Jr -- McCosker, J -- McDiarmid, R W -- McGuire, J -- Miller, M J -- Mooi, R -- Mooi, R D -- Moritz, C -- Myers, P -- Nachman, M W -- Nussbaum, R A -- Foighil, D O -- Parenti, L R -- Parham, J F -- Paul, E -- Paulay, G -- Perez-Eman, J -- Perez-Matus, A -- Poe, S -- Pogonoski, J -- Rabosky, D L -- Randall, J E -- Reimer, J D -- Robertson, D R -- Rodel, M-O -- Rodrigues, M T -- Roopnarine, P -- Ruber, L -- Ryan, M J -- Sheldon, F -- Shinohara, G -- Short, A -- Simison, W B -- Smith-Vaniz, W F -- Springer, V G -- Stiassny, M -- Tello, J G -- Thompson, C W -- Trnski, T -- Tucker, P -- Valqui, T -- Vecchione, M -- Verheyen, E -- Wainwright, P C -- Wheeler, T A -- White, W T -- Will, K -- Williams, J T -- Williams, G -- Wilson, E O -- Winker, K -- Winterbottom, R -- Witt, C C -- New York, N.Y. -- Science. 2014 May 23;344(6186):814-5. doi: 10.1126/science.344.6186.814.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉California Academy of Sciences, San Francisco, CA 94118, USA. LRocha@calacademy.org. ; Museu Paraense Emilio Goeldi, Belem, PA, 66040-170, Brazil. ; Western Australian Museum, Perth, WA, 6986, Australia. ; California Academy of Sciences, San Francisco, CA 94118, USA. ; Smithsonian Institution, Washington, DC 20560, USA. ; Natural History Museum, London, SW7 5BD, UK. ; Field Museum of Natural History, Chicago, IL 60605, USA. ; Villanova University, Villanova, PA 19085, USA. ; University of Milano-Bicocca, Milan, 20126, Italy. ; Utica College, Utica, NY 13502, USA. ; King Abdullah University of Science and Technology, Thuwal, 23955, Saudi Arabia. ; Universidad de Costa Rica, San Jose, 11501-2060, Costa Rica. ; University of California, Berkeley, CA 94720-3161, USA. ; University of Kansas, Lawrence, KS 66045, USA. ; Universidad de los Andes, Bogota, 4976, Colombia. ; Old Dominion University, Norfolk, VA 23529, USA. ; Museu Nacional de Historia Natural e da Ciencia, Lisbon, 7005-638, Portugal. ; Louisiana State University, Baton Rouge, LA 70803, USA. ; James Cook University, Townsville, 4811, Australia. ; University of Auckland, Auckland, 1142, New Zealand. ; NOAA Systematics Laboratory, Washington, DC 20013, USA. ; University of Chicago, Chicago, IL 60637, USA. ; American Museum of Natural History, New York, NY 10024, USA. ; Universidade de Sao Paulo, Sao Paulo, SP, 05508-090, Brazil. ; Universidade Federal do Rio de Janeiro, Macae, RJ, 27965-045, Brazil. ; University of California, Davis, CA 95616, USA. ; Conservation International, Denpasar, Bali, 80235, Indonesia. ; University of Nevada, Reno, NV 89557-0314, USA. ; Natural History Museum of Denmark, Copenhagen, DK-2100, Denmark. ; Museum National d'Histoire Naturelle, Paris, 75005, France. ; Addis Ababa University, Addis Ababa, 1176, Ethiopia. ; University of Sydney, Sydney, NSW, 2006, Australia. ; Museum Victoria, Melbourne, 3001, VIC, Australia. ; University of Colorado, Boulder, CO 80309-0334, USA. ; Harvard University, Cambridge, MA 02138, USA. ; Smithsonian Institution, Washington, DC 20560, USA. National University of Singapore, 117543, Singapore. ; Museum and Art Gallery of the Northern Territory, Darwin, 0820, NT, Australia. ; CSIRO Marine & Atmospheric Research, Hobart, TAS, 7000, Australia. ; Australian Museum, Sydney, NSW, 2010, Australia. ; Smithsonian Tropical Research Institute, Balboa, 0843-03092, Panama. ; Cornell University, Ithaca, NY 14853, USA. ; Universite Marien Ngouabi, Brazzaville, B.P. 69, Republic of Congo. ; National Museum of Nature and Science, Tsukuba, 305-0005, Japan. ; University of Wisconsin-Parkside, Kenosha, WI 53141-2000, USA. ; Cincinnati Museum Center, Cincinnati, OH 45203, USA. ; The Manitoba Museum, Winnipeg, MB, R3B 0N2, Canada. ; Australian National University, Canberra, ACT, 0200, Australia. ; University of Michigan, Ann Arbor, MI 48109-1079, USA. ; California State University, Fullerton, CA 92831, USA. ; The Ornithological Council, Chevy Chase, MD 20815, USA. ; University of Florida, Gainesville, fl32611, USA. ; Universidad Central de Venezuela, Caracas, 1041, Venezuela. ; Pontif cia Universidad Catolica de Chile, Santiago 6513677, Chile. ; University of New Mexico, Albuquerque, NM 87131-0001, USA. ; Bernice P. Bishop Museum, Honolulu, HI 96817, USA. ; University of the Ryukyus, Nishihara, 903-0213, Japan. ; Museum fur Naturkunde, Berlin, 10115, Germany. ; Naturhistorisches Museum der Burgergemeinde Bern, Bern, CH-3005, Switzerland. ; American Museum of Natural History, New York, NY 10024, USA. Long Island University, Brooklyn, NY 11201-8423, USA. ; Auckland Museum, Auckland, 1142, New Zealand. ; Centro de Ornitologia y Biodiversidad, Lima, 33, Peru. ; Royal Belgian Institute of Natural Sciences, Brussels, 1000, Belgium. ; McGill University, Montreal, QC, H9X 3V9, Canada. ; University of Alaska Museum, Fairbanks, AK 99775, USA. ; Royal Ontario Museum, Toronto, ON, M5S 2C6, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24855245" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biology/*methods ; Classification/*methods ; *Endangered Species ; *Extinction, Biological
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Unknown
    American Association for the Advancement of Science (AAAS)
    Publication Date: 2013-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bowie, James U -- R01GM063919/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Jan 25;339(6118):398-9. doi: 10.1126/science.1228655.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, Los Angeles, CA 90095, USA. bowie@mbi.ucla.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23349275" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/*chemistry ; Hydrogen Bonding ; Lipid Bilayers/chemistry ; Membrane Proteins/*chemistry ; Models, Molecular ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Subunits/chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2022-05-25
    Description: Author Posting. © American Geophysical Union, 2005. This article is posted here by permission of American Geophysical Union for personal use, not for redistribution. The definitive version was published in Global Biogeochemical Cycles 19 (2005): GB4006, doi:10.1029/2004GB002445.
    Description: We report iron measurements for water column and aerosol samples collected in the Sargasso Sea during July-August 2003 (summer 2003) and April-May 2004 (spring 2004). Our data reveal a large seasonal change in the dissolved iron (dFe) concentration of surface waters in the Bermuda Atlantic Time-series Study region, from ∼1–2 nM in summer 2003, when aerosol iron concentrations were high (mean 10 nmol m−3), to ∼0.1–0.2 nM in spring 2004, when aerosol iron concentrations were low (mean 0.64 nmol m−3). During summer 2003, we observed an increase of ∼0.6 nM in surface water dFe concentrations over 13 days, presumably due to eolian iron input; an estimate of total iron deposition over this same period suggests an effective solubility of 3–30% for aerosol iron. Our summer 2003 water column profiles show potentially growth-limiting dFe concentrations (0.02–0.19 nM) coinciding with a deep chlorophyll maximum at 100–150 m depth, where phytoplankton biomass is typically dominated by Prochlorococcus during late summer.
    Description: Funding for this work was provided by the U.S. National Science Foundation (OCE-0222053 to P. N. S., OCE-0222046 to T. M. C., and OCE-0241310 to D. J. M.), the U.S. National Aeronautics and Space Administration (NAG5-11265 to D. J. M.), the Australian Research Council (DP0342826 to A. R. B.), the Antarctic Climate and Ecosystems Cooperative Research Center, and the H. Unger Vetlesen Foundation.
    Keywords: Atmospheric deposition ; Iron ; Sargasso Sea
    Repository Name: Woods Hole Open Access Server
    Type: Article
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  • 10
    Publication Date: 2022-05-25
    Description: Author Posting. © The Author(s), 2011. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution. The definitive version was published in Deep Sea Research Part II: Topical Studies in Oceanography 58 (2011): 2094-2112, doi:10.1016/j.dsr2.2011.05.027.
    Description: This paper presents iron (Fe) profiles in the upper 1000 m from nine short-term (transect) stations and three long-term (process) stations occupied in the Australian sector of the Southern Ocean during the SAZ-Sense expedition in austral summer (January–February) 2007. Strong vertical and horizontal gradients in Fe concentrations were observed between the 18 sampled profiles (i.e. 0.09–0.63 nmol/l dissolved Fe (dFe)). Average dFe concentrations in surface waters in the northern Sub-Antarctic Zone (SAZ-N) West (station P1) were 0.27±0.04 nmol/l. This is lower than in the SAZ-N East region (station P3 and around) where average dFe values in the mixed layer were 0.48±0.10 nmol/l. The Polar Front (PF) station (P2) exhibited the lowest average surface Fe values (i.e. 0.22±0.02 nmol/l). Iron concentrations in deep waters down to 1000 m were more uniform (0.25–0.37 nmol/l dFe), which is in accordance with values reported elsewhere in remote waters of the Southern Ocean, but lower than those observed in the North Atlantic and North Pacific basins. A strong decoupling was observed between dFe and nutrient cycles at all stations. Particulate Fe levels were generally very low for all SAZ stations (〈0.08 – 1.38 nmol/l), with higher values observed at stations collected near Tasmania and in the SAZ-N East region. The intrusion of subtropical waters, enriched with Fe from sediments or dust further north, is thought to mediate Fe input to the SAZ-N and STZ areas, while input from below would be the main source of Fe in the PF region. We applied the tracer Fe* (Fe*= [dFe]-RFe:P × [PO4 3-], where RFe:P is the algal uptake ratio) to estimate the degree to which the water masses were Fe limited. In this study, Fe* tended to be negative and decreased with increasing depths and latitude. Positive Fe* values, indicating Fe sufficiency, were observed in the (near-)surface waters collected in the SAZ-N East and near continental sources, where primary production was higher and ultimately limited by the lack of macro-nutrients, not Fe. Micro-organisms residing in the SAZ-N West and PF on the other hand experienced negative Fe*, indicating a strong co-limitation by low silicic acid concentration and Fe supply (and light in the case of PF).
    Description: This research was supported by the Belgian Federal Science Policy Office (contracts SD/CA/03A, OA/00/025), the Australian Government Cooperative Research Centres Program through the Antarctic Climate and Ecosystems CRC (ACE CRC) and Australian Antarctic Science project #2720.
    Keywords: Iron ; Distributions ; Macro-nutrients ; Biogeochemistry ; Southern Ocean
    Repository Name: Woods Hole Open Access Server
    Type: Preprint
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