Liao G L, Palmer G
Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005-1892, USA.
Biochemistry. 1998 Nov 3;37(44):15583-92. doi: 10.1021/bi981476m.
Diazene reacts rapidly with cytochrome c oxidase to reduce cytochrome a and CuA and to form a charge-transfer complex with ferric cytochrome a3; the diazene may serve to bridge the heme iron of this cytochrome and CuB. The complex is characterized by an intense, optically active absorbance located at 847 nm. A similar band had been observed previously upon reduction of cytochrome oxidase with hydrazine [Markossian, K. A., Paitian, N. A., and Nalbandyan, R. M. (1983) FEBS Lett. 156, 235-238], but it appears that this band is actually due to the diazene produced as a result of the oxidation of the hydrazine that occurs in this process. A similar diazene to iron charge-transfer band is found following the reaction of diazene with ferric horseradish peroxidase and with hemin chloride but not with met-myoglobin.
重氮化合物与细胞色素c氧化酶迅速反应，以还原细胞色素a和CuA，并与高铁细胞色素a3形成电荷转移复合物；重氮化合物可能用于连接该细胞色素的血红素铁和CuB。该复合物的特征是在847nm处有强烈的、具有光学活性的吸光度。先前在用肼还原细胞色素氧化酶时也观察到了类似的谱带[Markossian, K. A., Paitian, N. A., and Nalbandyan, R. M. (1983) FEBS Lett. 156, 235 - 238]，但似乎该谱带实际上是由于在此过程中肼氧化产生的重氮化合物所致。在重氮化合物与高铁辣根过氧化物酶以及与氯化血红素反应后也发现了类似的重氮化合物与铁的电荷转移谱带，但与高铁肌红蛋白反应时未发现。
