Marine Biology

, Volume 154, Issue 3, pp 413–422

Flux capacities and acclimation costs in Trichodesmium from the Gulf of Mexico

  • Christopher M. Brown
  • James D. MacKinnon
  • Amanda M. Cockshutt
  • Tracy A. Villareal
  • Douglas A. Campbell
Research Article

DOI: 10.1007/s00227-008-0933-z

Cite this article as:
Brown, C.M., MacKinnon, J.D., Cockshutt, A.M. et al. Mar Biol (2008) 154: 413. doi:10.1007/s00227-008-0933-z

Abstract

Phytoplankton function and acclimation are driven by catalytic protein complexes that mediate key physiological transformations, including generation of photosynthetic ATP and reductant, and carbon and nitrogen fixation. Quantitation of capacities for these processes allows estimation of rates for key ecosystem processes, and identification of factors limiting primary productivity. We herein present molar quantitations of PSI, PSII, ATP synthase, RuBisCO and the Fe protein of nitrogenase of Trichodesmium collected from the Gulf of Mexico, in comparison to determinations for a range of cyanobacteria growing in culture. Using these measurements, estimates were generated for Trichodesmium capacities for carbon fixation of 1–3.4 g C g chl a−1 h−1 and nitrogen fixation of 0.06–0.17 g N g chl a−1 h−1, with diel variations in capacities. ATP synthase levels show that ATP synthesis capacity is sufficient to support these levels of carbon and nitrogen fixation, and that ATP synthase levels change over the day in accordance with the ATP demands of nitrogenase and RuBisCO activity. Levels of measured complexes indicate that Trichodesmium manifests n-type diel light acclimation through rapid changes in RuBisCO:PSII, supported by significant investment of cellular nitrogen. The plasticity in the levels and stoichiometry of these core complexes show that changes in the abundance of core protein complexes are an important component of acclimation and regulation of metabolic function by Trichodesmium populations.

Supplementary material

227_2008_933_MOESM1_ESM.doc (58 kb)
Electronic supplementary materials (DOC 57 kb)
227_2008_933_MOESM2_ESM.tif (95 kb)
Fig. S.1 (TIF 95.3 kb)
227_2008_933_MOESM3_ESM.tif (299 kb)
Fig. S.2 (TIF 299 kb)
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Fig. S.3 (TIF 278 kb)

Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  • Christopher M. Brown
    • 1
    • 2
  • James D. MacKinnon
    • 2
  • Amanda M. Cockshutt
    • 2
  • Tracy A. Villareal
    • 3
  • Douglas A. Campbell
    • 2
  1. 1.Department of BiologyUniversity of New BrunswickFrederictonCanada
  2. 2.Department of BiologyMount Allison UniversitySackvilleCanada
  3. 3.Marine Science InstituteThe University of Texas at AustinPort AransasUSA

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