The influence of chelating agents upon the dissimilatory reduction of Fe(III) by Shewanella putrefaciens. Part 2. Oxo- and hydroxo-bridged polynuclear Fe(III) complexes

Dobbin, Paul S., Requena Burmeister, Laura M., Heath, Sarah L., Powell, Anne K., McEwan, Alastair G. and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 (1996) The influence of chelating agents upon the dissimilatory reduction of Fe(III) by Shewanella putrefaciens. Part 2. Oxo- and hydroxo-bridged polynuclear Fe(III) complexes. BioMetals, 9 (3). pp. 291-301. ISSN 0966-0844

Full text not available from this repository. (Request a copy)

Abstract

The susceptibility to dissimilatory reduction of polynuclear oxo- and hydroxo-bridged Fe(m) complexes by Shewanella putrefaciens intact cells and membranes has been investigated. These complexes were ligated by the potential tetradentates heidi (H3heidi = N-(2-hydroxyethyl)iminodiacetic acid) or nta (H3nta = nitrilotriacetic acid), or the potential tridentate ida (H2ida = iminodiacetic acid). A number of defined small complexes with varied nuclearity and solubility properties were employed, as well as undefined species prepared by mixing different molar ratios of ida or heidi : Fe(III) in solution. The rates of Fe(III) reduction determined by an assay for Fe(II) formation with ferrozine were validated by monitoring c-type cytochrome oxidation and re-reduction associated with electron transport. For the undefined Fe(III)) polymeric species, reduction rates in whole cells and membranes were considerably faster in the presence of heidi compared to ida. This is believed to result from generally smaller and more reactive clusters forming with heidi as a consequence of the alkoxo function of this ligand being able to bridge between Fe(III) nuclei, with access to an Fe(III)) reductase located at the cytoplasmic membrane being of some importance. The increases in reduction rates of the undefined ida species with Fe(III) using membranes relative to whole cells reinforce such a view. Using soluble synthetic Fe(III) clusters, slow reduction was noted for an ore-bridged dimer coordinatively saturated with ida and featuring unligated carboxylates. This suggests that sterically hindering the cation can influence enzyme action. A heidi dimer and a heidi multimer (17 or 19 Fe(III)) nuclei), which are both of poor solubility, were found to be reduced by whole cells, but dissimilation rates increased markedly using membranes. These data suggest that Fe(III) reductase activity may be located at both the outer membrane and the cytoplasmic membrane of S. putrefaciens. Slower reduction of the heidi multimer relative to the heidi dimer reflects the presence of a central hydroxo(oxo)-bridged core containing nine Fe(III) nuclei within the former cluster. This unit is a poor substrate for dissimilation, owing to the fact that the Fe(III)) is not ligated by aminocarboxylate. The faster reduction noted for the heidi dimer in membranes than for a soluble ida monomer suggests that the presence of ligating water molecules may relieve steric hindrance to enzyme attack. Furthermore, reduction of an insoluble oxo-bridged nta dimer featuring ligating water molecules in intact cells was faster than that of a soluble monomer coordinatively saturated by nta and possessing an unligated carboxylate. This suggests that steric factors may override solubility considerations with respect to the susceptibility to reduction of certain Fe(III) complexes by the bacterium.

Item Type: Article
Uncontrolled Keywords: dissimilatory fe(iii) reduction,membrane-bound fe(iii) reductase,polynuclear fe(iii) complexes,shewanella putrefaciens,biomaterials,biochemistry, genetics and molecular biology(all),agricultural and biological sciences(all),metals and alloys ,/dk/atira/pure/subjectarea/asjc/2500/2502
Faculty \ School:
Faculty of Science > School of Biological Sciences
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 14 Jul 2022 16:31
Last Modified: 12 Aug 2022 05:35
URI: https://ueaeprints.uea.ac.uk/id/eprint/86138
DOI: 10.1007/BF00817930

Actions (login required)

View Item View Item