Gaul D F, Davidson M W, Palmer G, Shaw R W, Knaff D B
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock 79409.
Biochim Biophys Acta. 1988 Apr 14;953(3):226-31. doi: 10.1016/0167-4838(88)90029-5.
Magnetic circular dichroism spectra were obtained for the oxidized and reduced forms of cyanide, azide and carbon monoxide complexes of an O2-binding hemeprotein isolated from the photosynthetic purple sulfur bacterium, Chronatium vinosum. Cyanide binding to the protein, which results in formation of a low-spin complex, was highly pH dependent with little complex formation observed at pH values near or below 7.
从光合紫色硫细菌嗜硫红假单胞菌中分离出的一种与氧结合的血红素蛋白的氰化物、叠氮化物和一氧化碳配合物的氧化态和还原态的磁圆二色光谱已被测定。氰化物与该蛋白的结合会导致形成低自旋配合物，这种结合高度依赖于pH值，在pH值接近或低于7时几乎观察不到配合物的形成。
