Protein-protein recognition in biological systems exhibiting highly-conserved tertiary structure: cytochrome P450
Protein tertiary structure is more conserved than amino acid sequence, leading to a diverse range of functions observed in the same fold. Despite < 20 % overall sequence identity, cytochromes P450 all have the same fold. Bacterial Class I P450s receive electrons from a highly specific, often unidentified, ferredoxin, in which case the hemoprotein is termed “orphaned”.
CYP199A2, a Class I P450, accepts electrons from ferredoxins Pux and HaPux. Five orientation-dependent and one or...Expand abstract
- Publication date:
- Type of award:
- Level of award:
- Awarding institution:
- University of Oxford
- Local pid:
- Deposit date:
- Copyright holder:
- Eachan Oliver Daniel Johnson
- Copyright date:
- This thesis is not currently available in ORA.
If you are the owner of this record, you can report an update to it here: Report update to this record