An overview of technologies for immobilization of enzymes and surface analysis techniques for immobilized enzymes

NR Mohamad, NHC Marzuki, NA Buang… - Biotechnology & …, 2015 - Taylor & Francis
The current demands of sustainable green methodologies have increased the use of
enzymatic technology in industrial processes. Employment of enzyme as biocatalysts offers …

[PDF][PDF] The use of circular dichroism spectroscopy to study protein folding, form and function

DHA Corrêa, CHI Ramos - African Journal of Biochemistry …, 2009 - researchgate.net
Circular Dichroism (CD) is a spectroscopic technique widely used for the evaluation of the
conformation and stability of proteins in several environmental conditions like temperature …

Evolution of mammalian diving capacity traced by myoglobin net surface charge

S Mirceta, AV Signore, JM Burns, AR Cossins… - Science, 2013 - science.org
Introduction Evolution of extended breath-hold endurance enables the exploitation of the
aquatic niche by numerous mammalian lineages and is accomplished by elevated body …

Photocatalytic C–O Coupling Enzymes That Operate via Intramolecular Electron Transfer

J Lee, WJ Song - Journal of the American Chemical Society, 2023 - ACS Publications
Efficient and environmentally friendly conversion of light energy for direct utilization in
chemical production has been a long-standing goal in enzyme design. Herein, we …

Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins

DA Landfried, DA Vuletich, MP Pond, JTJ Lecomte - Gene, 2007 - Elsevier
The binding of a cofactor to a protein matrix often involves a reorganization of the
polypeptide structure. b Hemoproteins provide multiple examples of this behavior. In this …

Towards a “Golden Standard” for computing globin stability: Stability and structure sensitivity of myoglobin mutants

KP Kepp - Biochimica et Biophysica Acta (BBA)-Proteins and …, 2015 - Elsevier
Fast and accurate computation of protein stability is increasingly important for eg protein
engineering and protein misfolding diseases, but no consensus methods exist for important …

Peroxidase activity of myoglobin variants reconstituted with artificial cofactors

C Guo, RJ Chadwick, A Foulis, G Bedendi… - …, 2022 - Wiley Online Library
Myoglobin (Mb) can react with hydrogen peroxide (H2O2) to form a highly active
intermediate compound and catalyse oxidation reactions. To enhance this activity, known as …

Positively selected sites in cetacean myoglobins contribute to protein stability

P Dasmeh, AWR Serohijos, KP Kepp… - PLoS computational …, 2013 - journals.plos.org
Since divergence∼ 50 Ma ago from their terrestrial ancestors, cetaceans underwent a
series of adaptations such as a∼ 10–20 fold increase in myoglobin (Mb) concentration in …

Engineered myoglobin as a catalyst for atom transfer radical cyclisation

A Lubskyy, C Guo, RJ Chadwick, A Petri-Fink… - Chemical …, 2022 - pubs.rsc.org
Myoglobin was subjected to site-directed mutagenesis and transformed into a catalyst able
to perform atom transfer radical cyclisation reactions, ie intramolecular atom transfer radical …

Circular dichroism and site-directed spin labeling reveal structural and dynamical features of high-pressure states of myoglobin

MT Lerch, J Horwitz, J McCoy… - Proceedings of the …, 2013 - National Acad Sciences
Excited states of proteins may play important roles in function, yet are difficult to study
spectroscopically because of their sparse population. High hydrostatic pressure increases …