Using Tryptophan Mutants To Probe the Structural and Functional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis

Biochemistry ◽  
2017 ◽  
Vol 56 (48) ◽  
pp. 6355-6367 ◽  
Author(s):  
Shina Hussain ◽  
Diann Andrews ◽  
Bruce C. Hill
Keyword(s):  
Bacillus Subtilis ◽  
Cytochrome C ◽  
Functional Status ◽  
Cytochrome C Oxidase ◽  
Copper Binding

Exposure of Bacillus subtilis to silver inhibits activity of cytochrome c oxidase in vivo via interaction with SCO, the CuA assembly protein

Metallomics ◽  
2018 ◽  
Vol 10 (5) ◽  
pp. 735-744 ◽  
Author(s):  
Shina Hussain ◽  
Diann Andrews ◽  
Bruce C. Hill
Keyword(s):  
Bacillus Subtilis ◽  
Cytochrome C ◽  
Antimicrobial Agent ◽  
Cytochrome C Oxidase ◽  
Medicinal Use

Silver has long been used as an antimicrobial agent in general and medicinal use.

scholarly journals What Role Does COA6 Play in Cytochrome C Oxidase Biogenesis: A Metallochaperone or Thiol Oxidoreductase, or Both?

2020 ◽  
Vol 21 (19) ◽  
pp. 6983
Author(s):  
Shadi Maghool ◽  
Michael T. Ryan ◽  
Megan J. Maher
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Molecular Mechanisms ◽  
Intermembrane Space ◽  
Copper Binding ◽  
Transport Chain ◽  
Assembly Factor ◽  
Controversial Area ◽  
Thiol Oxidoreductase ◽  
Assembly Activity

Complex IV (cytochrome c oxidase; COX) is the terminal complex of the mitochondrial electron transport chain. Copper is essential for COX assembly, activity, and stability, and is incorporated into the dinuclear CuA and mononuclear CuB sites. Multiple assembly factors play roles in the biogenesis of these sites within COX and the failure of this intricate process, such as through mutations to these factors, disrupts COX assembly and activity. Various studies over the last ten years have revealed that the assembly factor COA6, a small intermembrane space-located protein with a twin CX9C motif, plays a role in the biogenesis of the CuA site. However, how COA6 and its copper binding properties contribute to the assembly of this site has been a controversial area of research. In this review, we summarize our current understanding of the molecular mechanisms by which COA6 participates in COX biogenesis.

scholarly journals Redox-regulated dynamic interplay between Cox19 and the copper-binding protein Cox11 in the intermembrane space of mitochondria facilitates biogenesis of cytochrome c oxidase

2015 ◽  
Vol 26 (13) ◽  
pp. 2385-2401 ◽  
Author(s):  
Manuela Bode ◽  
Michael W. Woellhaf ◽  
Maria Bohnert ◽  
Martin van der Laan ◽  
Frederik Sommer ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Specific Binding ◽  
Hydrophobic Surface ◽  
Cysteine Residue ◽  
Oxidative Modification ◽  
Intermembrane Space ◽  
Copper Binding ◽  
C Protein ◽  
Copper Transfer

Members of the twin Cx9C protein family constitute the largest group of proteins in the intermembrane space (IMS) of mitochondria. Despite their conserved nature and their essential role in the biogenesis of the respiratory chain, the molecular function of twin Cx9C proteins is largely unknown. We performed a SILAC-based quantitative proteomic analysis to identify interaction partners of the conserved twin Cx9C protein Cox19. We found that Cox19 interacts in a dynamic manner with Cox11, a copper transfer protein that facilitates metalation of the Cu(B) center of subunit 1 of cytochrome c oxidase. The interaction with Cox11 is critical for the stable accumulation of Cox19 in mitochondria. Cox19 consists of a helical hairpin structure that forms a hydrophobic surface characterized by two highly conserved tyrosine-leucine dipeptides. These residues are essential for Cox19 function and its specific binding to a cysteine-containing sequence in Cox11. Our observations suggest that an oxidative modification of this cysteine residue of Cox11 stimulates Cox19 binding, pointing to a redox-regulated interplay of Cox19 and Cox11 that is critical for copper transfer in the IMS and thus for biogenesis of cytochrome c oxidase.

Loss of function of Sco1 and its interaction with cytochrome c oxidase

2009 ◽  
Vol 296 (5) ◽  
pp. C1218-C1226 ◽  
Author(s):  
Lukas Stiburek ◽  
Katerina Vesela ◽  
Hana Hansikova ◽  
Helena Hulkova ◽  
Jiri Zeman
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Copper Homeostasis ◽  
Copper Binding ◽  
Loss Of Function ◽  
Muscle Mitochondria ◽  
Juxtamembrane Region ◽  
Cellular Copper ◽  
The Impact ◽  
Blue Native

Sco1 and Sco2 are mitochondrial copper-binding proteins involved in the biogenesis of the CuA site in the cytochrome c oxidase (CcO) subunit Cox2 and in the maintenance of cellular copper homeostasis. Human Surf1 is a CcO assembly factor with an important but poorly characterized role in CcO biogenesis. Here, we analyzed the impact on CcO assembly and tissue copper levels of a G132S mutation in the juxtamembrane region of SCO1 metallochaperone associated with early onset hypertrophic cardiomyopathy, encephalopathy, hypotonia, and hepatopathy, assessed the total copper content of various SURF1 and SCO2-deficient tissues, and investigated the possible physical association between CcO and Sco1. The steady-state level of mutant Sco1 was severely decreased in the muscle mitochondria of the SCO1 patient, indicating compromised stability and thus loss of function of the protein. Unlike the wild-type variant, residual mutant Sco1 appeared to migrate exclusively in the monomeric form on blue native gels. Both the activity and content of CcO were reduced in the patient's muscle to ∼10–20% of control values. SCO1-deficient mitochondria showed accumulation of two Cox2 subcomplexes, suggesting that Sco1 is very likely responsible for a different posttranslational aspect of Cox2 maturation than Sco2. Intriguingly, the various SURF1-deficient samples analyzed showed a tissue-specific copper deficiency similar to that of SCO-deficient samples, suggesting a role for Surf1 in copper homeostasis regulation. Finally, both blue native immunoblot analysis and coimmunoprecipitation revealed that a fraction of Sco1 physically associates with the CcO complex in human muscle mitochondria, suggesting a possible direct relationship between CcO and the regulation of cellular copper homeostasis.

scholarly journals Electrochemical recognition and quantification of cytochrome c expression in Bacillus subtilis and aerobe/anaerobe Escherichia coli using N,N,N′,N′-tetramethyl-para-phenylene-diamine (TMPD)

2017 ◽  
Vol 8 (11) ◽  
pp. 7682-7688 ◽  
Author(s):  
S. Kuss ◽  
E. E. L. Tanner ◽  
M. Ordovas-Montanes ◽  
R. G. Compton
Keyword(s):  
Escherichia Coli ◽  
Bacillus Subtilis ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Quantitative Detection ◽  
Oxidase Test ◽  
Electrochemical Recognition ◽  
Phenylene Diamine

Transferring the colorimetric oxidase test to electrochemistry: quantitative detection of bacteria by means of cytochrome c oxidase.

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