Pistorius E K, Gewitz H S, Voss H, Vennesland B
Biochim Biophys Acta. 1977 Apr 12;481(2):384-91. doi: 10.1016/0005-2744(77)90272-8.
The formation of HCN from D-histidine in Chlorella vulgaris extracts is shown to be due to the combined action of a soluble protein and a particulate component. Either horse-radish peroxidase (EC 1.11.1.7) or a metal ion with redox properties can be substituted for the particulate component. Ions of manganese and vanadium are especially effective, as are o-phenanthroline complexes of iron. Cobalt ions are less active. The D-amino acid oxidase (EC 1.4.3.3) from kidney and the L-amino acid oxidase (EC 1.4.3.2) from snake venom likewise cause HCN production from histidine when supplemented with the particulate preparation from Chlorella or with peroxidase or with a redox metal ion. The stereospecificity of the amino acid oxidase determines which of the two stereoisomers of histidine is active as an HCN precursor. Though histidine is the best substrate for HCN production, other naturally occurring aromatic amino acids (viz. tyrosine, phenylalanine and tryptophan) can also serve as HCN precursors with these enzyme systems. The relative effectiveness of each substrate varies with the amino acid oxidase enzyme and with the supplement. With respect to this latter property, the particulate preparation from Chlorella behaves more like a metal ion than like peroxidase.
在小球藻提取物中，由D-组氨酸形成HCN被证明是由于一种可溶性蛋白质和一种颗粒成分的共同作用。辣根过氧化物酶（EC 1.11.1.7）或具有氧化还原特性的金属离子可以替代颗粒成分。锰离子和钒离子特别有效，铁的邻菲罗啉配合物也是如此。钴离子活性较低。来自肾脏的D-氨基酸氧化酶（EC 1.4.3.3）和来自蛇毒的L-氨基酸氧化酶（EC 1.4.3.2），当补充小球藻的颗粒制剂、过氧化物酶或氧化还原金属离子时，同样会导致组氨酸产生HCN。氨基酸氧化酶的立体特异性决定了组氨酸的两种立体异构体中哪一种作为HCN前体具有活性。尽管组氨酸是产生HCN的最佳底物，但其他天然存在的芳香族氨基酸（即酪氨酸、苯丙氨酸和色氨酸）也可以作为这些酶系统的HCN前体。每种底物的相对有效性随氨基酸氧化酶和补充剂的不同而变化。就后一种特性而言，小球藻的颗粒制剂表现得更像金属离子而不是过氧化物酶。
