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Thesis

Protein-protein recognition in biological systems exhibiting highly-conserved tertiary structure: cytochrome P450

Abstract:

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...

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Institution:
University of Oxford
Research group:
Bioinorganic Chemistry
Oxford college:
New College
Department:
Mathematical,Physical & Life Sciences Division - Chemistry - Inorganic Chemistry Laboratory
Role:
Author

Contributors

Role:
Supervisor
Publication date:
2013
Type of award:
DPhil
Level of award:
Doctoral
URN:
uuid:d19f5f52-d1ce-4ec2-be83-fd52f01124f8
Local pid:
ora:9035

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