Anderson R F, Patel K B, Adams G E
Int J Radiat Biol Relat Stud Phys Chem Med. 1977 Dec;32(6):523-31. doi: 10.1080/09553007714551311.
The enzyme D-amino acid oxidase and its apoenzyme have been irradiated at pH 5.5--10 under conditions designed to assess the inactivating effect of OH radicals and the selective free radicals Br2- and (SCN)2-. Near neutral pH, removal of the coenzyme FAD from the enzyme results in greater inactivation by selective free-radical attack. From pulse-radiolysis spectra, this increase is associated with attack on tyrosine and tryptophan residues in the protein. A large increase in inactivation of both the haloenzyme and apoenzyme by selective free-radical attack is seen with increasing alkalinity. This is consistent with attack on tyrosine being of major importance.
在旨在评估羟基自由基以及选择性自由基Br2-和(SCN)2-的灭活作用的条件下，对D-氨基酸氧化酶及其脱辅基酶在pH 5.5至10的环境中进行了辐照。在接近中性pH值时，从酶中去除辅酶FAD会导致选择性自由基攻击引起的更大程度的失活。从脉冲辐解光谱来看，这种增加与蛋白质中酪氨酸和色氨酸残基受到的攻击有关。随着碱性增强，卤化酶和脱辅基酶因选择性自由基攻击而导致的失活大幅增加。这与酪氨酸受到的攻击起主要作用是一致的。
