HR: 16:45h
AN: B24A-04 INVITED [Abstracts]
TI: Chemolithoautotrophy and its Relation to Magnetism and Biomineralization in Marine Magnetotactic
Bacteria
AU: * Bazylinski, D A
EM: dbazylin@iastate.edu
AF: Iowa State University, Department of BBMB
207 Science I, Ames, IA 50011
United States
AU: Williams, T J
EM: tijawi@iastate.edu
AF: Iowa State University, Department of BBMB
207 Science I, Ames, IA 50011
United States
AU: Zhang, C L
EM: Zhang@srel.edu
AF: University of Georgia, Savannah River Ecology Laboratory, Drawer E, Aiken, SC 29802
United States
AU: Scott, J H
EM: j.scott@gl.ciw.edu
AF: Carnegie Inst. of Washington, Geophysical Laboratory
5251 Broad Branch Rd. NW, Washington, DC 20015
United States
AB:
All cultured, marine, magnetite-producing, magnetotactic bacteria (MB) are capable of chemolithoautotrophy and use a number
of electron donors to support this mode of growth including reduced sulfur compounds. Several vibrioid strains are known to
rely on the Calvin-Benson-Bassham (CBB) cycle for autotrophy. An obligately microaerophilic, magnetite-producing, coccoid
strain (MC-1) grew with sulfide and thiosulfate as electron donors and 14C-labelling experiments showed that virtually
all cell C was derived from H14CO3-/14CO2 confirming autotrophy in this strain. Cell-free extracts
of strain MC-1 did not exhibit ribulose-1,5-bisphosphate carboxylase-oxygenase (RubisCO) activity and nor were RubisCO genes
found in the draft genome of the organism. Cell extracts also did not exhibit carbon monoxide dehydrogenase activity
indicating that the acetyl-CoA pathway also does not function in strain MC-1. The 13C content of whole cells of strain
MC-1 relative to the 13C content of the H14CO3-/14CO2 used for growth
(Δδ13C) was -11.4 ppt. Cellular fatty acids showed enrichment of 13C relative to biomass. Activities
for three key enzymes of the reverse or reductive tricarboxylic acid (rTCA) cycle were demonstrated for MC-1: fumarate
reductase, pyruvate: acceptor oxidoreductase and 2-oxoglutarate: acceptor oxidoreductase. Although ATP citrate lyase (another
key enzyme of the rTCA cycle) activity was not detected in cell-free extracts of strain MC-1 using commonly used assays for
this enzyme, cell-free extract was found to rapidly cleave citrate, and the reaction was dependent upon the presence of ATP,
coenzyme A and NADH. Thus, we infer the presence of an ATP-dependent citrate-cleaving enzyme or enzymes. The
Δδ13C value and results from enzyme studies are consistent with the operation of the rTCA cycle for
autotrophy in strain MC-1. Strain MC-1 appears to be the first known member of the alpha-Proteobacteria to assimilate
CO2 during autotrophic growth using the rTCA cycle. Based on the type of chemolithoautotrophy described above, it is
clear why marine magnetite-producing MB occupy a precise location, the oxic-anoxic interface, in vertical chemical gradients
within chemically-stratified coastal environments: they must have an electron donor, sulfide and perhaps others, and an
electron acceptor, O2. The presumed function of magnetosomes is that the magnetic dipole resulting from the magnetosomes
aids the cell in locating and maintaining an optimal position within vertical chemical gradients. MB process large amounts
of Fe in the biomineralization of magnetosomes: cells consist of 1-3% Fe (dry wt). Because of this, and the fact that many
chemolithoautotrophic, non-magnetotactic bacteria occupy a similar niche, we have been investigating possible physiological
reasons for the production of magnetosomes and the processing of such large amounts of Fe. We have found that some marine
vibrioid strains grow in O2-gradient medium with Fe(II) as the electron donor. Cells appear to oxidize the Fe(II) and
produce a layer of Fe oxyhydroxides within the gradient suggesting that cells obtain energy from the oxidation of Fe(II).
DE: 0419 Biomineralization
DE: 0428 Carbon cycling (4806)
DE: 0463 Microbe/mineral interactions
DE: 0465 Microbiology: ecology, physiology and genomics (4840)
DE: 0471 Oxidation/reduction reactions (4851)
SC: Biogeosciences [B]
MN: Fall Meeting 2005