Department of Chemistry, The University of Arizona, Tucson, Arizona 85721.
Plant Physiol. 1974 Jan;53(1):39-44. doi: 10.1104/pp.53.1.39.
The properties of a form of ribulose diphosphate carboxylase having a high affinity for CO(2) have been studied. Its apparent Km(HCO(3) (-)) of 0.5 to 0.8 mm (pH 7.8) and calculated Km(CO(2)) of 11 to 18 mum are comparable to the values exhibited by intact chloroplasts during photosynthesis. This form of the enzyme was released from chloroplasts in hypotonic media and was unstable, rapidly converting to a form having a high Km(HCO(3) (-)) of 20 to 25 mm similar to that for the purified enzyme. Incubation of the enzyme with MgCl(2) and HCO(3) (-) yielded a third form with an intermediate Km(HCO(3) (-)) of 2.5 to 3.0 mm.The low Km form had sufficient activity both at air levels of CO(2) and at saturating CO(2) to account for the rates of photosynthesis by intact chloroplasts. The low Km form could be stabilized in the presence of ribose 5-phosphate, adenosine triphosphate, and MgCl(2), at low temperatures for up to 2 hours.
已经研究了一种具有高亲和力的二磷酸核酮糖羧化酶形式的性质。其对HCO3-(pH7.8)的表观Km(0.5 至 0.8mm)和计算出的对 CO2 的 Km(11 至 18μm)与光合作用期间完整叶绿体表现出的数值相当。这种形式的酶从低渗介质中的叶绿体中释放出来,并且不稳定,迅速转化为具有高 Km(HCO3-)的形式,为 20 至 25mm,类似于纯化酶的形式。用 MgCl2 和 HCO3-孵育酶会产生 Km(HCO3-)中间值为 2.5 至 3.0mm 的第三种形式。低 Km 形式在空气中 CO2 水平和饱和 CO2 水平下均具有足够的活性,足以说明完整叶绿体的光合作用速率。在存在核糖 5-磷酸、三磷酸腺苷和 MgCl2 的情况下,低 Km 形式可以在低温下稳定长达 2 小时。