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https://hdl.handle.net/1822/45778
Título: | Activity-stability relationships revisited in blue oxidases catalyzing electron transfer at extreme temperatures |
Autor(es): | Roulling, Frédéric Godin, Amandine Cipolla, Alexandre Collins, Tony Miyazaki, Kentaro Feller, Georges |
Palavras-chave: | Enzyme Stability Oxidoreductases Pseudoalteromonas Adaptation, Physiological Electron Transport Multicopper oxidase Cuproxidase Psychrophiles Thermophiles Electron transfer |
Data: | Set-2016 |
Editora: | Springer Verlag |
Revista: | Extremophiles |
Citação: | Roulling F., Godin A., Cipolla A., Collins T., Miyazaki K. and Feller G. (2016). Activity–stability relationships revisited in blue oxidases catalyzing electron transfer at extreme temperatures. Extremophiles, 20(5):621-9. DOI 10.1007/s00792-016-0851-9. |
Resumo(s): | Cuproxidases are a subset of the blue multicopper oxidases that catalyze the oxidation of toxic Cu(I) ions into less harmful Cu(II) in the bacterial periplasm. Cuproxidases from psychrophilic, mesophilic, and thermophilic bacteria display the canonical features of temperature adaptation, such as increases in structural stability and apparent optimal temperature for activity with environmental temperature as well as increases in the binding affinity for catalytic and substrate copper ions. In contrast, the oxidative activities at 25 °C for both the psychrophilic and thermophilic enzymes are similar, suggesting that the nearly temperature-independent electron transfer rate does not require peculiar adjustments. Furthermore, the structural flexibilities of both the psychrophilic and thermophilic enzymes are also similar, indicating that the firm and precise bindings of the four catalytic copper ions are essential for the oxidase function. These results show that the requirements for enzymatic electron transfer, in the absence of the selective pressure of temperature on electron transfer rates, produce a specific adaptive pattern, which is distinct from that observed in enzymes possessing a well-defined active site and relying on conformational changes such as for the induced fit mechanism. |
Tipo: | Artigo |
Descrição: | The online version of this article (doi:10.1007/s00792-016-0851-9) contains supplementary material, which is available to authorized users. |
URI: | https://hdl.handle.net/1822/45778 |
DOI: | 10.1007/s00792-016-0851-9 |
ISSN: | 1431-0651 |
e-ISSN: | 1433-4909 |
Versão da editora: | https://link.springer.com/article/10.1007/s00792-016-0851-9 |
Arbitragem científica: | yes |
Acesso: | Acesso restrito UMinho |
Aparece nas coleções: | DBio - Artigos/Papers |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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Roulling et al 2016 Final Published Paper.pdf Acesso restrito! | 1,08 MB | Adobe PDF | Ver/Abrir |