Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases
Dye-decolorizing peroxidases (DyPs) are heme-containing enzymes that are structurally unrelated to other peroxidases. Some DyPs show high potential for applications in biotechnology, which critically depends on the stability and redox potential (E°') of the enzyme. Here we provide a comparative...
| Main Authors: | , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Elsevier
2024-01-01
|
| Series: | BBA Advances |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2667160323000418 |
| _version_ | 1827223316425867264 |
|---|---|
| author | Catarina Barbosa Carolina F. Rodrigues Nikola Lončar Lígia O. Martins Smilja Todorovic Célia M. Silveira |
| author_facet | Catarina Barbosa Carolina F. Rodrigues Nikola Lončar Lígia O. Martins Smilja Todorovic Célia M. Silveira |
| author_sort | Catarina Barbosa |
| collection | DOAJ |
| description | Dye-decolorizing peroxidases (DyPs) are heme-containing enzymes that are structurally unrelated to other peroxidases. Some DyPs show high potential for applications in biotechnology, which critically depends on the stability and redox potential (E°') of the enzyme. Here we provide a comparative analysis of UV–Vis- and surface-enhanced resonance Raman-based spectroelectrochemical methods for determination of the E°' of DyPs from two different organisms, and their variants generated targeting E°' upshift. We show that substituting the highly conserved Arginine in the distal side of the heme pocket by hydrophobic amino acid residues impacts the heme architecture and redox potential of DyPs from the two organisms in a very distinct manner. We demonstrate the advantages and drawbacks of the used spectroelectrochemical approaches, which is relevant for other heme proteins that contain multiple heme centers or spin populations. |
| first_indexed | 2024-03-08T18:18:51Z |
| format | Article |
| id | doaj.art-b461941d27d843be938ad3b87cd3b552 |
| institution | Directory Open Access Journal |
| issn | 2667-1603 |
| language | English |
| last_indexed | 2025-03-21T16:52:27Z |
| publishDate | 2024-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | BBA Advances |
| spelling | doaj.art-b461941d27d843be938ad3b87cd3b5522024-06-15T06:14:27ZengElsevierBBA Advances2667-16032024-01-015100112Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidasesCatarina Barbosa0Carolina F. Rodrigues1Nikola Lončar2Lígia O. Martins3Smilja Todorovic4Célia M. Silveira5Instituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Oeiras 2780-157, PortugalInstituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Oeiras 2780-157, PortugalGecco Biotech, Nijenborgh 4, Groningen 9747AG, the NetherlandsInstituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Oeiras 2780-157, PortugalInstituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Oeiras 2780-157, PortugalInstituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Av. da República, Oeiras 2780-157, Portugal; Corresponding author.Dye-decolorizing peroxidases (DyPs) are heme-containing enzymes that are structurally unrelated to other peroxidases. Some DyPs show high potential for applications in biotechnology, which critically depends on the stability and redox potential (E°') of the enzyme. Here we provide a comparative analysis of UV–Vis- and surface-enhanced resonance Raman-based spectroelectrochemical methods for determination of the E°' of DyPs from two different organisms, and their variants generated targeting E°' upshift. We show that substituting the highly conserved Arginine in the distal side of the heme pocket by hydrophobic amino acid residues impacts the heme architecture and redox potential of DyPs from the two organisms in a very distinct manner. We demonstrate the advantages and drawbacks of the used spectroelectrochemical approaches, which is relevant for other heme proteins that contain multiple heme centers or spin populations.http://www.sciencedirect.com/science/article/pii/S2667160323000418Heme proteinsRedox potentialSpectroelectrochemistryDye decolorizing peroxidases |
| spellingShingle | Catarina Barbosa Carolina F. Rodrigues Nikola Lončar Lígia O. Martins Smilja Todorovic Célia M. Silveira Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases BBA Advances Heme proteins Redox potential Spectroelectrochemistry Dye decolorizing peroxidases |
| title | Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases |
| title_full | Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases |
| title_fullStr | Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases |
| title_full_unstemmed | Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases |
| title_short | Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases |
| title_sort | spectroelectrochemistry for determination of the redox potential in heme enzymes dye decolorizing peroxidases |
| topic | Heme proteins Redox potential Spectroelectrochemistry Dye decolorizing peroxidases |
| url | http://www.sciencedirect.com/science/article/pii/S2667160323000418 |
| work_keys_str_mv | AT catarinabarbosa spectroelectrochemistryfordeterminationoftheredoxpotentialinhemeenzymesdyedecolorizingperoxidases AT carolinafrodrigues spectroelectrochemistryfordeterminationoftheredoxpotentialinhemeenzymesdyedecolorizingperoxidases AT nikolaloncar spectroelectrochemistryfordeterminationoftheredoxpotentialinhemeenzymesdyedecolorizingperoxidases AT ligiaomartins spectroelectrochemistryfordeterminationoftheredoxpotentialinhemeenzymesdyedecolorizingperoxidases AT smiljatodorovic spectroelectrochemistryfordeterminationoftheredoxpotentialinhemeenzymesdyedecolorizingperoxidases AT celiamsilveira spectroelectrochemistryfordeterminationoftheredoxpotentialinhemeenzymesdyedecolorizingperoxidases |