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- Heel, Thomas, et al. Show all 3 Authors
- BBA - Proteins and Proteomics 2013 v.1834 pp. 1539-1544
- Humicola insolens; Trichoderma reesei; cellulases; circular dichroism spectroscopy; cysteine; disulfide bonds; feedstocks; fuels; fungi; heat inactivation; heat treatment; lignocellulose; pH; protein engineering; temperature; thermal stability
- ... Numerous protein engineering studies have focused on increasing the thermostability of fungal cellulases to improve production of fuels and chemicals from lignocellulosic feedstocks. However, the engineered enzymes still undergo thermal inactivation at temperatures well below the inactivation temperatures of hyperthermophilic cellulases. In this report, we investigated the role of free cysteines i ...
- Heel, Thomas, et al. Show all 5 Authors
- Journal of the American Chemical Society 2015 v.137 no.43 pp. 13861-13865
- Sulfolobus; active sites; catalytic activity; crystal structure; cysteine; cytochrome P-450; enzyme stability; heme; heme iron; histidine; ligands; mutants; mutation; protein structure; serine; thermal stability
- ... Almost all known members of the cytochrome P450 (CYP) superfamily conserve a key cysteine residue that coordinates the heme iron. Although mutation of this residue abolishes monooxygenase activity, recent work has shown that mutation to either serine or histidine unlocks non-natural carbene- and nitrene-transfer activities. Here we present the first crystal structure of a histidine-ligated P450. T ...
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