isoform HRP C, dramatic enhancement of radical stability by retaining 41% of its initial activity in conditions when wild-type is completely inactivated
loss of a structural restraint in the proximal heme pocket that allows slippage of the proximal heme ligand, but only in the reduced state. This is a remarkably subtle and specific effect that appears to increase the flexibility of the reduced state of the mutant compared to that of the wild-type protein. Significant change in the Fe2+/Fe3+ redox potential of the mutant T171S
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.2fold higher than the wild-type value
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.1fold lower than the wild-type value
formation of styrene epoxide is 2.7fold higher as compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme
formation of styrene epoxide is 2.9fold higher as compared to wild-type enzyme. Protein melting temperature is 2.3°C higher as compared to wild-type enzyme. Mutant is separated into two distinct bands during chromatofocusing. The first band contains predominantly low spin protein, and the second band contains predominantly high spin protein
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
formation of styrene epoxide is 2.7fold higher as compared to wild-type enzyme. Protein melting temperature is 1.6°C lower compared to wild-type enzyme
kcat/Km for Reactive Black 5 is decreased, kcat/KM for veratryl alcohol is increased slightly. kcat/KM for Mn2+ as substrate is 1.5fold lower than the wild-type value
mutant enzyme is completely unable to oxidize both veratryl, alcohol and Reactive Black 5. kcat/KM for Mn2+ as substrate is 1.6fold higher than the wild-type value
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
formation of styrene epoxide is 1.4fold higher as compared to wild-type enzyme. Protein melting temperature is 3.5°C higher as compared to wild-type enzyme
the mutant enzyme shows an important red-shift of their fluorescence maximum, along with an increased shoulder at 396 nm, significant alteration in the protein structure, causing some of the tryptophan residues to become more solvent accessible
the QPO null mutant shows an oxidative stress phenotype, suggesting that QPO plays a certain role in scavenging endogenously generated reactive oxygen species
the QPO null mutant shows an oxidative stress phenotype, suggesting that QPO plays a certain role in scavenging endogenously generated reactive oxygen species
the QPO null mutant shows an oxidative stress phenotype, suggesting that QPO plays a certain role in scavenging endogenously generated reactive oxygen species
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
application of maximum likelihood methods to infer an amino acid sequence consistent with the most recent common ancestor of plant peroxidases, the grandparent, and cloning and expression in Escherichia coli