The 2.0Å Resolution Structure of the Catalytic Portion of a Cyanobacterial Membrane-bound Manganese Superoxide Dismutase

Atzenhofer, Werner; Regelsberger, Günther; Jacob, Uwe; Peschek, Günter A.; Furtmüller, Paul G.; Huber, Robert; Obinger, Christian

doi:10.1016/s0022-2836(02)00624-1

Cited by 39 publications

(41 citation statements)

References 34 publications

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“…Seven structures of MnSODs have been reported, three of which are tetrameric [human MnSOD (Borgstahl et al, 1992), Thermus thermophilus MnSOD (Ludwig et al, 1991) and Aspergillus fumigatus MnSOD (Fluckiger et al, 2002)], while the others are dimeric [Escherichia coli MnSOD (Edwards et al, 1998), Bacillus stearothermophilus MnSOD (Parker & Blake, 1988), Bacillus anthracis MnSOD (Boucher et al, 2005), Deinococcus radiodurans MnSOD (Dennis et al, 2006) and cyanobacterium MnSOD (Atzenhofer et al, 2002)]. All the structures share a common overall fold with the ironcontaining enzymes.…”

Section: Resultsmentioning

confidence: 99%

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Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

et al. 2008

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PDB References: manganese superoxide dismutase 3dc6, r3dc6sf; 3dc5, r3dc5sf. Caenorhabditis elegans expresses two manganese superoxide dismutase enzymes (MnSOD-2 and MnSOD-3) that are targeted to the mitochondrion. MnSOD-2 is constitutively expressed, while synthesis of MnSOD-3 is inducible. The structures of these two mononuclear metalloenzymes have been determined to 1.8 and 1.7 Å resolution, respectively. Pink crystals formed in space group P4 1 2 1 2 for each, with unit-cell parameters a = b = 81.0, c = 137.4 Å for MnSOD-2 and a = b = 81.8, c = 136.0 Å for MnSOD-3. The final structure of MnSOD-3 was refined to R = 21.6% and R free = 26.2% at 293 K, and R = 18.9% and R free = 22.6% at 100 K, while that of MnSOD-2 was refined to R = 16.9% and R free = 20.1% at 100 K. The asymmetric unit cell is comprised of two subunits. The resulting structures are very similar to that of human MnSOD and form a tetramer corresponding to a dimer of dimers. The subunit interface between dimers is comprised of two four-helix bundles that stabilize the biologically significant homotetramer.

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Section: Resultsmentioning

confidence: 99%

“…MnSOD-3 has a deletion of three amino acids (Ala147-Thr149; Fig. 2a) compared with other MnSODs apart than that from the cyanobacterium Anabaena variabilis (Atzenhofer et al, 2002). This deletion results in the loss of an -helical region ( 7; Fig.…”

Section: Resultsmentioning

confidence: 99%

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

et al. 2008

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“…As well a CuZnSOD was identified in the marine cyanobacterium Synechococcus WH7803 (45). X-ray crystallography was performed for the FeSOD of T. elongatus (46) and the MnSOD of Nostoc PCC 7120 (8). Table II lists twelve cyanobacterial species or strains where sequences of the whole or nearly complete genome are available.…”

Section: Discussionmentioning

confidence: 99%

“…MnSOD is localized in both cytoplasmic and thylakoid membranes (2). Recently, the 2.0-Å structure of the catalytic portion of the MnSOD was reported (8). Membrane attachment of Nostoc MnSOD was confirmed by immunoblotting and activity staining (9).…”

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The Iron Superoxide Dismutase from the Filamentous Cyanobacterium Nostoc PCC 7120

Regelsberger

Laaha

Dietmann

et al. 2004

Journal of Biological Chemistry

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The nitrogen-fixing filamentous cyanobacterium Nostoc PCC 7120 (formerly named Anabaena PCC 7120) possesses two genes for superoxide dismutase, a unique membrane-associated manganese superoxide dismutase (MnSOD) and a soluble iron superoxide dismutase (FeSOD). A phylogenetic analysis of FeSODs shows that cyanobacterial enzymes form a well separated cluster with filamentous species found in one subcluster and unicellular species in the other. Activity staining, inhibition patterns, and immunogold labeling show that FeSOD is localized in the cytosol of vegetative cells and heterocysts (nitrogenase containing specialized cells formed during nitrogen-limiting conditions). The recombinant Nostoc FeSOD is a homodimeric, acidic enzyme exhibiting the characteristic iron peak at 350 nm in its ferric state, an almost 100% occupancy of iron per subunit, a specific activity using the ferricytochrome assay of (2040 ؎ 90) units mg ؊1 at pH 7.8, and a dissociation constant K d of the azide-FeSOD complex of 2.1 mM. Using stopped flow spectroscopy it was shown that the decay of superoxide in the presence of various FeSOD concentrations is first-order in enzyme concentration allowing the calculation of the catalytic rate constants, which increase with decreasing pH: 5.3 ؋ 10 9 M ؊1 s ؊1 (pH 7) to 4.8 ؋ 10 6 M ؊1 s ؊1 (pH 10). FeSOD and MnSOD complement each other to keep the superoxide level low in Nostoc PCC 7120, which is discussed with respect to the fact that Nostoc PCC 7120 exhibits oxygenic photosynthesis and oxygen-dependent respiration within a single prokaryotic cell and also has the ability to form differentiated cells under nitrogen-limiting conditions.

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“…radiodurans (pdb code 1Y67), 24 and the filamentous cyanobacterium Anabena PCC 7120 (pdb code 1GV3) 25 gave an rmsd of ~0.4-0.7 Å for the monomer, and ~0.5-0.9 Å for the dimer (Figure 4). Figure 5A).…”

Section: Crystal Structure Of Mnsod1mentioning

confidence: 99%

Identification of Manganese Superoxide Dismutase from Sphingobacterium sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation

et al. 2015

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Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work of researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-forprofit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. Publisher's statement:This document is the Accepted Manuscript version of a Published Work that appeared in final form in ACS Chemical Biology, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see: http://dx.doi.org/10.1021/acschembio.5b00298The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP url' above for details on accessing the published version and note that access may require a subscription. centre ligated by three His, one Asp and a water/hydroxide in each active site. We propose that the lignin oxidation reactivity of these enzymes is due to the production of hydroxyl radical, a highly reactive oxidant. This is the first demonstration that MnSOD is a microbial lignin-oxidising enzyme.3

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The 2.0Å Resolution Structure of the Catalytic Portion of a Cyanobacterial Membrane-bound Manganese Superoxide Dismutase

Cited by 39 publications

References 34 publications

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

Purification, crystallization and X-ray structures of the two manganese superoxide dismutases fromCaenorhabditis elegans

The Iron Superoxide Dismutase from the Filamentous Cyanobacterium Nostoc PCC 7120

Identification of Manganese Superoxide Dismutase from Sphingobacterium sp. T2 as a Novel Bacterial Enzyme for Lignin Oxidation

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