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Stability/activity tradeoffs in Thermus thermophilus HB27 laccase

Shin, Jieun and Gray, Harry B. and Winkler, Jay R. (2020) Stability/activity tradeoffs in Thermus thermophilus HB27 laccase. Journal of Biological Inorganic Chemistry, 25 (3). pp. 233-238. ISSN 0949-8257. PMCID PMC7085441. doi:10.1007/s00775-020-01754-7. https://resolver.caltech.edu/CaltechAUTHORS:20200123-100835510

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Abstract

We report the temperature dependence of the formal potential of type 1 copper (Cu_(T1)) in Thermusthermophilus HB27 laccase. Employing [Ru(NH₃)₄ (bpy)](PF₆)₂ (0.505 vs. NHE) as the redox titrant, we found that the Cu_(T1)^(2+/+) potential decreased from approximately 480 to 420 mV (vs. NHE) as the temperature was raised from 20 to 65 °C. Of importance is that the ΔS_(rc)° of − 120 J mol⁻¹ K⁻¹ is substantially more negative than those for other blue copper proteins. We suggest that the highly unfavorable reduction entropy is attributable to Cu_(T1) inaccessibility to the aqueous medium. Although the active site residues are buried, which is critical for maintaining thermostability, the flexibility around Cu_(T1) is maintained, allowing enzyme activity at ambient temperature.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1007/s00775-020-01754-7DOIArticle
https://rdcu.be/b0GmvPublisherFree ReadCube access
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7085441/PubMed CentralArticle
ORCID:
AuthorORCID
Gray, Harry B.0000-0002-7937-7876
Winkler, Jay R.0000-0002-4453-9716
Alternate Title:Stability/activity tradeoffs in Thermusthermophilus HB27 laccase
Additional Information:© 2020 Society for Biological Inorganic Chemistry (SBIC). Received: 4 November 2019; Accepted: 25 December 2019. First Online: 22 January 2020. Research reported in this publication was supported by the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health under award number R01DK019038. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. Additional support for this research was provided by the Arnold and Mabel Beckman Foundation.
Funders:
Funding AgencyGrant Number
NIHR01DK019038
Arnold and Mabel Beckman FoundationUNSPECIFIED
Subject Keywords:Electron transfer; Thermodynamics; Thermophile
Issue or Number:3
PubMed Central ID:PMC7085441
DOI:10.1007/s00775-020-01754-7
Record Number:CaltechAUTHORS:20200123-100835510
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20200123-100835510
Official Citation:Shin, J., Gray, H.B. & Winkler, J.R. Stability/activity tradeoffs in Thermusthermophilus HB27 laccase. J Biol Inorg Chem 25, 233–238 (2020). https://doi.org/10.1007/s00775-020-01754-7
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:100871
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:23 Jan 2020 18:19
Last Modified:09 Feb 2022 23:16

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