
Vanadium Requirements and Uptake Kinetics in the Dinitrogen-Fixing Bacterium Azotobacter vinelandii
Author(s) -
JeanPhilippe Bellenger,
Thomas Wichard,
Anne M. L. Kraepiel
Publication year - 2008
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.02236-07
Subject(s) - azotobacter vinelandii , siderophore , catechol , nitrogenase , bacteria , chemistry , azotobacter chroococcum , azotobacteraceae , vanadium , biochemistry , cofactor , strain (injury) , diazotroph , enzyme , biology , inorganic chemistry , nitrogen fixation , genetics , anatomy , gene
Vanadium is a cofactor in the alternative V-nitrogenase that is expressed by some N(2)-fixing bacteria when Mo is not available. We investigated the V requirements, the kinetics of V uptake, and the production of catechol compounds across a range of concentrations of vanadium in diazotrophic cultures of the soil bacterium Azotobacter vinelandii. In strain CA11.70, a mutant that expresses only the V-nitrogenase, V concentrations in the medium between 10(-8) and 10(-6) M sustain maximum growth rates; they are limiting below this range and toxic above. A. vinelandii excretes in its growth medium micromolar concentrations of the catechol siderophores azotochelin and protochelin, which bind the vanadate oxoanion. The production of catechols increases when V concentrations become toxic. Short-term uptake experiments with the radioactive isotope (49)V show that bacteria take up the V-catechol complexes through a regulated transport system(s), which shuts down at high V concentrations. The modulation of the excretion of catechols and of the uptake of the V-catechol complexes allows A. vinelandii to precisely manage its V homeostasis over a range of V concentrations, from limiting to toxic.