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Allostery in Callinectes sapidus hemocyanin: cooperative oxygen binding and interactions with L-lactate, calcium, and protons

Cite this: Biochemistry 1988, 27, 6, 1995–2001
Publication Date (Print):March 22, 1988
https://doi.org/10.1021/bi00406a028
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    Cited By

    This article is cited by 20 publications.

    1. Edward I. Solomon, David E. Heppner, Esther M. Johnston, Jake W. Ginsbach, Jordi Cirera, Munzarin Qayyum, Matthew T. Kieber-Emmons, Christian H. Kjaergaard, Ryan G. Hadt, and Li Tian . Copper Active Sites in Biology. Chemical Reviews 2014, 114 (7) , 3659-3853. https://doi.org/10.1021/cr400327t
    2. Michael A. Menze,, Nadja Hellmann,, Heinz Decker, and, Manfred K. Grieshaber. Allosteric Models for Multimeric Proteins:  Oxygen-Linked Effector Binding in Hemocyanin. Biochemistry 2005, 44 (30) , 10328-10338. https://doi.org/10.1021/bi050507s
    3. Christian Damsgaard, Angela Fago, Silke Hagner-Holler, Hans Malte, Thorsten Burmester, Roy E. Weber. Molecular and functional characterization of hemocyanin of the giant African millipede, Archispirostreptus gigas. Journal of Experimental Biology 2013, 201 https://doi.org/10.1242/jeb.080861
    4. N. Hellmann. Control of kinetics by cooperative interactions. IUBMB Life 2011, 63 (5) , 329-336. https://doi.org/10.1002/iub.459
    5. Shun Hirota, Naoki Tanaka, Ivan Mičetić, Paolo Di Muro, Satoshi Nagao, Hiroaki Kitagishi, Koji Kano, Richard S. Magliozzo, Jack Peisach, Mariano Beltramini, Luigi Bubacco. Structural Basis of the Lactate-dependent Allosteric Regulation of Oxygen Binding in Arthropod Hemocyanin. Journal of Biological Chemistry 2010, 285 (25) , 19338-19345. https://doi.org/10.1074/jbc.M109.076067
    6. N. Hellmann, M. Paoli, F. Giomi, M. Beltramini. Unusual oxygen binding behavior of a 24-meric crustacean hemocyanin. Archives of Biochemistry and Biophysics 2010, 495 (2) , 112-121. https://doi.org/10.1016/j.abb.2009.12.025
    7. Matthieu Bruneaux, Peran Terrier, Emmanuelle Leize, Jean Mary, François H. Lallier, Franck Zal. Structural study of Carcinus maenas hemocyanin by native ESI‐MS: Interaction with L ‐lactate and divalent cations. Proteins: Structure, Function, and Bioinformatics 2009, 77 (3) , 589-601. https://doi.org/10.1002/prot.22471
    8. Alessandra Olianas, Barbara Manconi, Daniela Masia, Maria T. Sanna, Massimo Castagnola, Susanna Salvadori, Irene Messana, Bruno Giardina, Mariagiuseppina Pellegrini. The oxygen-binding modulation of hemocyanin from the Southern spiny lobster Palinurus gilchristi. Journal of Comparative Physiology B 2009, 179 (2) , 193-203. https://doi.org/10.1007/s00360-008-0302-8
    9. Roy E. Weber, Jane W. Behrens, Hans Malte, Angela Fago. Thermodynamics of oxygenation-linked proton and lactate binding govern the temperature sensitivity of O2 binding in crustacean( Carcinus maenas ) hemocyanin. Journal of Experimental Biology 2008, 211 (7) , 1057-1062. https://doi.org/10.1242/jeb.013433
    10. Luca Ronda, Serena Faggiano, Stefano Bettati, Nadja Hellmann, Heinz Decker, Tilo Weidenbach, Andrea Mozzarelli. Hemocyanin from E. californicum encapsulated in silica gels: Oxygen binding and conformational states. Gene 2007, 398 (1-2) , 202-207. https://doi.org/10.1016/j.gene.2007.02.036
    11. Alessandra Olianas, Maria T. Sanna, Irene Messana, Massimo Castagnola, Daniela Masia, Barbara Manconi, Angelo Cau, Bruno Giardina, Mariagiuseppina Pellegrini. The Hemocyanin of the Shamefaced Crab Calappa granulata: Structural-Functional Characterization. The Journal of Biochemistry 2006, 139 (6) , 957-966. https://doi.org/10.1093/jb/mvj110
    12. Mariano Beltramini, Nadia Colangelo, Folco Giomi, Luigi Bubacco, Paolo Di Muro, Nadja Hellmann, Elmar Jaenicke, Heinz Decker. Quaternary structure and functional properties of Penaeus monodon hemocyanin. The FEBS Journal 2005, 272 (8) , 2060-2075. https://doi.org/10.1111/j.1742-4658.2005.04634.x
    13. Maria T. Sanna, Alessandra Olianas, Massimo Castagnola, Luigi Sollai, Barbara Manconi, Susanna Salvadori, Bruno Giardina, Mariagiuseppina Pellegrini. Oxygen-binding modulation of hemocyanin from the slipper lobster Scyllarides latus. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2004, 139 (2) , 261-268. https://doi.org/10.1016/j.cbpc.2004.08.005
    14. Nadja Hellmann. Bohr-effect and buffering capacity of hemocyanin from the tarantula E. californicum. Biophysical Chemistry 2004, 109 (1) , 157-167. https://doi.org/10.1016/j.bpc.2003.10.031
    15. Nadja Hellmann, Julia Hörnemann, Elmar Jaenicke, Heinz Decker. Urate as effector for crustacean hemocyanins. Micron 2004, 35 (1-2) , 109-110. https://doi.org/10.1016/j.micron.2003.10.038
    16. N. Hellmann, E. Jaenicke, H. Decker. Two types of urate binding sites on hemocyanin from the crayfish Astacus leptodactylus: an ITC study. Biophysical Chemistry 2001, 90 (3) , 279-299. https://doi.org/10.1016/S0301-4622(01)00150-8
    17. K.E. van Holde, Karen I. Miller. Hemocyanins. 1995, 1-81. https://doi.org/10.1016/S0065-3233(08)60545-8
    18. Nobuo Makino, Hiromi Ohnaka. Role of oligomeric interactions in the cooperativity of crayfish hemocyanin. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1993, 1162 (3) , 237-245. https://doi.org/10.1016/0167-4838(93)90287-2
    19. M. Brouwer. Oxygen Carriers as Molecular Models of Allosteric Behavior. 1992, 1-21. https://doi.org/10.1007/978-3-642-76418-9_1
    20. Heinz Decker, Reinhard Sterner. Nested allostery of arthropodan hemocyanin (Eurypelma californicum and Homarus americanus). Journal of Molecular Biology 1990, 211 (1) , 281-293. https://doi.org/10.1016/0022-2836(90)90027-J

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