Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase.
CPR (NADPH-cytochrome P450 reductase) is a multidomain protein containing two flavin-containing domains joined by a connecting domain thought to control the necessary movements of the catalytic domains during electronic cycles. We present a detailed biochemical analysis of two chimaeric CPRs compose...
| Main Authors: | , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2011
|
| _version_ | 1797106106270482432 |
|---|---|
| author | Aigrain, L Pompon, D Truan, G |
| author_facet | Aigrain, L Pompon, D Truan, G |
| author_sort | Aigrain, L |
| collection | OXFORD |
| description | CPR (NADPH-cytochrome P450 reductase) is a multidomain protein containing two flavin-containing domains joined by a connecting domain thought to control the necessary movements of the catalytic domains during electronic cycles. We present a detailed biochemical analysis of two chimaeric CPRs composed of the association of human or yeast FMN with the alternative connecting/FAD domains. Despite the assembly of domains having a relatively large evolutionary distance between them, our data support the idea that the integrity of the catalytic cycle is conserved in our chimaeric enzymes, whereas the recognition, interactions and positioning of both catalytic domains are probably modified. The main consequences of the chimaerogenesis are a decrease in the internal electron-transfer rate between both flavins correlated with changes in the geometry of chimaeric CPRs in solution. Results of the present study highlight the role of the linker and connecting domain in the recognition at the interfaces between the catalytic domains and the impact of interdomain interactions on the redox potentials of the flavins, the internal electron-transfer efficiency and the global conformation and dynamic equilibrium of the CPRs. |
| first_indexed | 2024-03-07T06:57:00Z |
| format | Journal article |
| id | oxford-uuid:fe759aa6-21a4-4115-b489-a3c1b747b42a |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:57:00Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | oxford-uuid:fe759aa6-21a4-4115-b489-a3c1b747b42a2022-03-27T13:36:40ZRole of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fe759aa6-21a4-4115-b489-a3c1b747b42aEnglishSymplectic Elements at Oxford2011Aigrain, LPompon, DTruan, GCPR (NADPH-cytochrome P450 reductase) is a multidomain protein containing two flavin-containing domains joined by a connecting domain thought to control the necessary movements of the catalytic domains during electronic cycles. We present a detailed biochemical analysis of two chimaeric CPRs composed of the association of human or yeast FMN with the alternative connecting/FAD domains. Despite the assembly of domains having a relatively large evolutionary distance between them, our data support the idea that the integrity of the catalytic cycle is conserved in our chimaeric enzymes, whereas the recognition, interactions and positioning of both catalytic domains are probably modified. The main consequences of the chimaerogenesis are a decrease in the internal electron-transfer rate between both flavins correlated with changes in the geometry of chimaeric CPRs in solution. Results of the present study highlight the role of the linker and connecting domain in the recognition at the interfaces between the catalytic domains and the impact of interdomain interactions on the redox potentials of the flavins, the internal electron-transfer efficiency and the global conformation and dynamic equilibrium of the CPRs. |
| spellingShingle | Aigrain, L Pompon, D Truan, G Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase. |
| title | Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase. |
| title_full | Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase. |
| title_fullStr | Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase. |
| title_full_unstemmed | Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase. |
| title_short | Role of the interface between the FMN and FAD domains in the control of redox potential and electronic transfer of NADPH-cytochrome P450 reductase. |
| title_sort | role of the interface between the fmn and fad domains in the control of redox potential and electronic transfer of nadph cytochrome p450 reductase |
| work_keys_str_mv | AT aigrainl roleoftheinterfacebetweenthefmnandfaddomainsinthecontrolofredoxpotentialandelectronictransferofnadphcytochromep450reductase AT pompond roleoftheinterfacebetweenthefmnandfaddomainsinthecontrolofredoxpotentialandelectronictransferofnadphcytochromep450reductase AT truang roleoftheinterfacebetweenthefmnandfaddomainsinthecontrolofredoxpotentialandelectronictransferofnadphcytochromep450reductase |