Mohr P, Kühn M, Wesuls E, Renneberg R, Scheller F
Acta Biol Med Ger. 1979;38(2-3):495-501.
The H2O2 dependent catalysis of cytochrome P-450 was compared with the catalytic mechanism of horse radish peroxidase, methemoglobin and iron protoporphyrin complexes. A relatively stable intermediate being comparable to compound I of horse radish peroxidase is formed in the case of iron porphyrin complexes, methemoglobin and probably cytochrome P-450. In the case of peroxidase compound II is the more stable intermediate. This could be the reason for the different catalytic properties of peroxidase on the one hand and iron porphyrin complexes, methemoglobin and cytochrome P-450 on the other hand.
将细胞色素P - 450的过氧化氢依赖性催化作用与辣根过氧化物酶、高铁血红蛋白和铁原卟啉复合物的催化机制进行了比较。在铁卟啉复合物、高铁血红蛋白以及可能的细胞色素P - 450的情况下，会形成一种相对稳定的中间体，其与辣根过氧化物酶的化合物I相当。在过氧化物酶的情况下，化合物II是更稳定的中间体。这可能是过氧化物酶与铁卟啉复合物、高铁血红蛋白和细胞色素P - 450在催化特性上存在差异的原因。
