Tryptophan extends the life of cytochrome P450.

ABSTRACT: Powerfully oxidizing enzymes need protective mechanisms to prevent self-destruction. The flavocytochrome P450 BM3 from Priestia megaterium (P450_BM3) is a self-sufficient monooxygenase that hydroxylates fatty acid substrates using O₂ and NADPH as co-substrates. Hydroxylation of long-chain fatty acids (≥C₁₄) is well coupled to O₂ and NADPH consumption, but shorter chains (≤C₁₂) are more poorly coupled. Hydroxylation of p-nitrophenoxydodecanoic acid by P450_BM3 produces a spectrophotometrically detectable product wherein the coupling of NADPH consumption to product formation is just 10%. Moreover, the rate of NADPH consumption is 1.8 times that of O₂ consumption, indicating that an oxidase uncoupling pat

SUBMITTER: Ravanfar R 

PROVIDER: S-EPMC10722969 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature