Kinetic, electrochemical and spectral characterization of bacterial and archaeal rusticyanins; unexpected stability issues and consequences for applications in biotechnology.

Autor: Wilson LA; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia., Melville JN; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia., Pedroso MM; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia., Krco S; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia., Hoelzle R; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia; Australian Centre for Ecogenomics, The University of Queensland, Brisbane, QLD 4072, Australia., Zaugg J; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia; Australian Centre for Ecogenomics, The University of Queensland, Brisbane, QLD 4072, Australia., Southam G; School of the Environment, The University of Queensland, Brisbane, QLD 4072, Australia., Virdis B; Australian Centre for Water and Environmental Biotechnology, The University of Queensland, Brisbane, QLD 4072, Australia., Evans P; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia; Australian Centre for Ecogenomics, The University of Queensland, Brisbane, QLD 4072, Australia., Supper J; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia; Australian Centre for Ecogenomics, The University of Queensland, Brisbane, QLD 4072, Australia., Harmer JR; Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane, QLD 4072, Australia., Tyson G; Centre for Microbiome Research, Queensland University of Technology, Woolloongabba, QLD 4102, Australia., Clark A; Sustainable Minerals Institute, The University of Queensland, Brisbane, QLD 4072, Australia., Schenk G; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia; Australian Centre for Ecogenomics, The University of Queensland, Brisbane, QLD 4072, Australia; Australian Institute for Bioengineering and Nanotechnology, The University of Queensland, Brisbane, QLD 4072, Australia; Sustainable Minerals Institute, The University of Queensland, Brisbane, QLD 4072, Australia. Electronic address: schenk@uq.edu.au., Bernhardt PV; School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD 4072, Australia. Electronic address: p.bernhardt@uq.edu.au.
Jazyk: angličtina
Zdroj: Journal of inorganic biochemistry [J Inorg Biochem] 2024 Jul; Vol. 256, pp. 112539. Date of Electronic Publication: 2024 Mar 25.
DOI: 10.1016/j.jinorgbio.2024.112539
Abstrakt: Motivated by the ambition to establish an enzyme-driven bioleaching pathway for copper extraction, properties of the Type-1 copper protein rusticyanin from Acidithiobacillus ferrooxidans (AfR) were compared with those from an ancestral form of this enzyme (N0) and an archaeal enzyme identified in Ferroplasma acidiphilum (FaR). While both N0 and FaR show redox potentials similar to that of AfR their electron transport rates were significantly slower. The lack of a correlation between the redox potentials and electron transfer rates indicates that AfR and its associated electron transfer chain evolved to specifically facilitate the efficient conversion of the energy of iron oxidation to ATP formation. In F. acidiphilum this pathway is not as efficient unless it is up-regulated by an as of yet unknown mechanism. In addition, while the electrochemical properties of AfR were consistent with previous data, previously unreported behavior was found leading to a form that is associated with a partially unfolded form of the protein. The cyclic voltammetry (CV) response of AfR immobilized onto an electrode showed limited stability, which may be connected to the presence of the partially unfolded state of this protein. Insights gained in this study may thus inform the engineering of optimized rusticyanin variants for bioleaching processes as well as enzyme-catalyzed solubilization of copper-containing ores such as chalcopyrite.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023. Published by Elsevier Inc.)
Databáze: MEDLINE
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