scholarly journals Absence of the iron-containing superoxide dismutase in mitochondria from mustard (Brassica campestris)

1981 ◽  
Vol 195 (1) ◽  
pp. 229-233 ◽  
Author(s):  
M L Salin ◽  
S M Bridges
Keyword(s):  
Superoxide Dismutase ◽  
Brassica Campestris ◽  
Polyacrylamide Gel ◽  
Superoxide Dismutases ◽  
Intermembrane Space ◽  
Mitochondrial Matrix ◽  
Mature Leaves ◽  
Etiolated Seedlings

Mitochondria were isolated from mature leaves as well as etiolated seedlings of Brassica campestris (mustard), a eukaryote previously shown to possess the iron-containing isoenzyme of superoxide dismutase. On the basis of KCN- and H2O2-sensitivity, and on polyacrylamide-gel analysis, only the cuprozinc and mangano superoxide dismutases were found in mitochondria. The iron-containing enzyme was absent. The mangano enzyme was found in the mitochondrial matrix, whereas the cuprozinc enzyme appeared to be localized in the intermembrane space.

scholarly journals Cmc1p Is a Conserved Mitochondrial Twin CX9C Protein Involved in Cytochrome c Oxidase Biogenesis

2008 ◽  
Vol 28 (13) ◽  
pp. 4354-4364 ◽  
Author(s):  
Darryl Horn ◽  
Hassan Al-Ali ◽  
Antoni Barrientos
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Superoxide Dismutase ◽  
Cytochrome C Oxidase ◽  
Mitochondrial Enzymes ◽  
Intermembrane Space ◽  
Mitochondrial Matrix ◽  
Copper Chaperones ◽  
Copper Trafficking ◽  
Mitochondrial Inner Membrane ◽  
Copper Incorporation

ABSTRACT Copper is an essential cofactor of two mitochondrial enzymes: cytochrome c oxidase (COX) and Cu-Zn superoxide dismutase (Sod1p). Copper incorporation into these enzymes is facilitated by metallochaperone proteins which probably use copper from a mitochondrial matrix-localized pool. Here we describe a novel conserved mitochondrial metallochaperone-like protein, Cmc1p, whose function affects both COX and Sod1p. In Saccharomyces cerevisiae, Cmc1p localizes to the mitochondrial inner membrane facing the intermembrane space. Cmc1p is essential for full expression of COX and respiration, contains a twin CX9C domain conserved in other COX assembly copper chaperones, and has the ability to bind copper(I). Additionally, mutant cmc1 cells display increased mitochondrial Sod1p activity, while CMC1 overexpression results in decreased Sod1p activity. Our results suggest that Cmc1p could play a direct or indirect role in copper trafficking and distribution to COX and Sod1p.

scholarly journals Intracellular localization, isolation and characterization of two distinct varieties of superoxide dismutase from Neurospora crassa

1980 ◽  
Vol 187 (2) ◽  
pp. 321-328 ◽  
Author(s):  
Landis E. A. Henry ◽  
Richard Cammack ◽  
Jean-Paul Schwitzguebel ◽  
John M. Palmer ◽  
David O. Hall
Keyword(s):  
Superoxide Dismutase ◽  
Neurospora Crassa ◽  
Analytical Ultracentrifugation ◽  
Intracellular Localization ◽  
Total Activity ◽  
Superoxide Dismutases ◽  
Intermembrane Space ◽  
Matrix Space ◽  
Isolation And Characterization ◽  
High Yields

1. Neurospora crassa was found to contain two distinct superoxide dismutases. 2. Most of the activity is associated with the cytosolic fraction and was shown to be the Cu/Zn-containing form of the protein. 3. Mitochondria isolated from Neurospora crassa showed two distinct superoxide dismutases: a cyanide-sensitive Cu/Zn-containing protein and a cyanide-insensitive form which probably contains manganese. 4. Localization experiments, using selective marker enzymes and digitonin fractionation, indicated that the cyanide-sensitive form is localized in the intermembrane space, whereas the cyanide-insensitive form is confined to the mitochondrial matrix space. 5. The cytosolic Cu/Zn-containing superoxide dismutase was isolated in high yields and extensively characterized by using e.p.r. spectroscopy, isoelectric focusing and analytical ultracentrifugation. 6. E.p.r. spectroscopy was used to monitor changes in the copper environment of the native protein after the addition of a number of potential inhibitors and after high-pH treatment. 7. Both of the cyanide-sensitive Cu/Zn-containing enzymes (cytosolic and mitochondrial) appeared to have identical properties which in turn were different from the cyanide-insensitive enzyme. 8. It is probable that the cyanide-insensitive enzyme was not previously detected, owing to its low amount (less than 10% of the total activity), greater lability than the cyanide-sensitive enzyme and the necessity of obtaining a mitochondrial-enriched fraction before its isolation.

scholarly journals Mitochondrial mislocalization and altered assembly of a cluster of Barth syndrome mutant tafazzins

2006 ◽  
Vol 174 (3) ◽  
pp. 379-390 ◽  
Author(s):  
Steven M. Claypool ◽  
J. Michael McCaffery ◽  
Carla M. Koehler
Keyword(s):  
Point Mutations ◽  
Mutant Gene ◽  
Barth Syndrome ◽  
Membrane Association ◽  
Intermembrane Space ◽  
Mitochondrial Matrix ◽  
Mitochondrial Membranes ◽  
Membrane Bilayer ◽  
Conserved Residues ◽  
Tm Domain

None of the 28 identified point mutations in tafazzin (Taz1p), which is the mutant gene product associated with Barth syndrome (BTHS), has a biochemical explanation. In this study, endogenous Taz1p was localized to mitochondria in association with both the inner and outer mitochondrial membranes facing the intermembrane space (IMS). Unexpectedly, Taz1p does not contain transmembrane (TM) segments. Instead, Taz1p membrane association involves a segment that integrates into, but not through, the membrane bilayer. Residues 215–232, which were predicted to be a TM domain, were identified as the interfacial membrane anchor by modeling four distinct BTHS mutations that occur at conserved residues within this segment. Each Taz1p mutant exhibits altered membrane association and is nonfunctional. However, the basis for Taz1p dysfunction falls into the following two categories: (1) mistargeting to the mitochondrial matrix or (2) correct localization associated with aberrant complex assembly. Thus, BTHS can be caused by mutations that alter Taz1p sorting and assembly within the mitochondrion, indicating that the lipid target of Taz1p is resident to IMS-facing leaflets.

Selective induction of manganous superoxide dismutase in human monocytes

1985 ◽  
Vol 249 (5) ◽  
pp. C393-C397 ◽  
Author(s):  
K. Asayama ◽  
R. L. Janco ◽  
I. M. Burr
Keyword(s):  
Superoxide Dismutase ◽  
Muramyl Dipeptide ◽  
Superoxide Production ◽  
Bacterial Lipopolysaccharide ◽  
Culture Period ◽  
Superoxide Dismutases ◽  
Minimal Effect ◽  
Human Monocytes ◽  
Transient Decrease ◽  
Copper Zinc

Radioimmunoassays for both human copper-zinc and manganous superoxide dismutases (Cu-Zn SOD and Mn SOD, respectively) have been developed, validated, and utilized to measure the concentrations of these enzymes in cultured monocytes. Monocyte Mn SOD increased 4.7-fold over basal during 3 days of culture, an increase that was markedly enhanced by stimulation with bacterial lipopolysaccharide (LPS). Cu-Zn SOD showed a transient decrease over the culture period but was unaffected by LPS. Stimulation with muramyl dipeptide had minimal effect on Mn SOD and no effect on Cu-Zn SOD during culture, even at a concentration capable of activating the monocytes, as defined by zymosan-induced superoxide production.

scholarly journals Potentiation of Antibiofilm Activity of Amphotericin B by Superoxide Dismutase Inhibition

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Katrijn De Brucker ◽  
Anna Bink ◽  
Els Meert ◽  
Bruno P. A. Cammue ◽  
Karin Thevissen
Keyword(s):  
Reactive Oxygen Species ◽  
Superoxide Dismutase ◽  
Candida Albicans ◽  
Amphotericin B ◽  
Reactive Oxygen ◽  
Intracellular Reactive Oxygen Species ◽  
Superoxide Dismutases ◽  
Antibiofilm Activity ◽  
Oxygen Species ◽  
Ammonium Tetrathiomolybdate

This study demonstrates a role for superoxide dismutases (Sods) in governing tolerance ofCandida albicansbiofilms to amphotericin B (AmB). Coincubation ofC. albicansbiofilms with AmB and the Sod inhibitors N,N′-diethyldithiocarbamate (DDC) or ammonium tetrathiomolybdate (ATM) resulted in reduced viable biofilm cells and increased intracellular reactive oxygen species levels as compared to incubation of biofilm cells with AmB, DDC, or ATM alone. Hence, Sod inhibitors can be used to potentiate the activity of AmB againstC. albicansbiofilms.

scholarly journals A Fraction of Yeast Cu,Zn-Superoxide Dismutase and Its Metallochaperone, CCS, Localize to the Intermembrane Space of Mitochondria

2001 ◽  
Vol 276 (41) ◽  
pp. 38084-38089 ◽  
Author(s):  
Lori A. Sturtz ◽  
Kerstin Diekert ◽  
Laran T. Jensen ◽  
Roland Lill ◽  
Valeria Cizewski Culotta
Keyword(s):  
Superoxide Dismutase ◽  
Intermembrane Space

scholarly journals Investigation of human erythrocyte superoxide dismutase by 1H nuclear-magnetic-resonance spectroscopy

1980 ◽  
Vol 185 (1) ◽  
pp. 245-252 ◽  
Author(s):  
H A O Hill ◽  
W K Lee ◽  
J V Bannister ◽  
W H Bannister
Keyword(s):  
Superoxide Dismutase ◽  
Active Site ◽  
Human Erythrocyte ◽  
Superoxide Dismutases ◽  
Resonance Spectroscopy ◽  
Structural Homology ◽  
Histidine Residues ◽  
Erythrocyte Superoxide Dismutase ◽  
1H Nuclear Magnetic Resonance ◽  
Acetyl Group

The 170MHZ 1 H n.m.r. spectra of the Cu(II)/Zn(II), Cu(I)/Zn(II) and apo- forms of human erythrocyte superoxide dismutase (EC 1.15.1.1) are reported. Resonances are assigned to the C-2 and C-4 protons of histidine residues in the active site, and it is suggested that five or six histidine residues serve as ligands to the metal ions in each subunit of the enzyme. The remaining assigned resonances are associated with histidine-41, N-terminal N-acetyl group, histidine- 108 and cysteine- 109. A comparison of the n.m.r. spectra of human and bovine superoxide dismutases suggests significant structural homology.

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