ArticleThe Journal of biological chemistry2010
An unconventional copper protein required for cytochrome c oxidase respiratory function under extreme acidic conditions.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 25 citations in OpenAlex.
- In Hyphomicrobium denitrificans Two Related Sulfane-Sulfur Responsive Transcriptional Repressors Regulate Thiosulfate Oxidation and Have a Deep Impact on Nitrate Respiration and Anaerobic Biosyntheses.Molecular microbiology · 2025Article
- Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features.Dalton transactions (Cambridge, England : 2003) · 2024Article
- Progress in bioleaching: fundamentals and mechanisms of microbial metal sulfide oxidation - part A.Applied microbiology and biotechnology · 2022Review
- Determinants of Copper Resistance inGenes · 2020Article
- Identification and Analysis of a Novel Gene Cluster Involves in FeCurrent microbiology · 2018Article
- Electron transfer in an acidophilic bacterium: interaction between a diheme cytochrome and a cupredoxin.Chemical science · 2018Article
- Microbial copper resistance: importance in biohydrometallurgy.Microbial biotechnology · 2017Review
- Cytoplasmic CopZ-Like Protein and Periplasmic Rusticyanin and AcoP Proteins as Possible Copper Resistance Determinants in Acidithiobacillus ferrooxidans ATCC 23270.Applied and environmental microbiology · 2016Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Very little is known about the processes used by acidophile organisms to preserve stability and function of respiratory pathways. Here, we reveal a potential strategy of these organisms for protecting and keeping functional key enzymes under extreme conditions. Using Acidithiobacillus ferrooxidans, we have identified a protein belonging to a new cupredoxin subfamily, AcoP, for "acidophile CcO partner," which is required for the cytochrome c oxidase (CcO) function. We show that it is a multifunctional copper protein with at least two roles as follows: (i) as a chaperone-like protein involved in the protection of the Cu(A) center of the CcO complex and (ii) as a linker between the periplasmic cytochrome c and the inner membrane cytochrome c oxidase. It could represent an interesting model for investigating the multifunctionality of proteins known to be crucial in pathways of energy metabolism.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.