Ontology highlight
ABSTRACT:
SUBMITTER: Orlando BJ
PROVIDER: S-EPMC4707933 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Orlando Benjamin J BJ Borbat Peter P PP Georgieva Elka R ER Freed Jack H JH Malkowski Michael G MG
Biochemistry 20151207 50
Cyclooxygenases (COXs) are heme-containing sequence homodimers that utilize tyrosyl radical-based catalysis to oxygenate substrates. Tyrosyl radicals are formed from a single turnover of substrate in the peroxidase active site generating an oxy-ferryl porphyrin cation radical intermediate that subsequently gives rise to a Tyr-385 radical in the cyclooxygenase active site and a Tyr-504 radical nearby. We have utilized double-quantum coherence (DQC) spectroscopy to determine the distance distribut ...[more]