Kobayashi K, Katsura E, Kondo T, Ishimoto M
J Biochem. 1978 Nov;84(5):1209-15. doi: 10.1093/oxfordjournals.jbchem.a132238.
Thiosulfate and sulfide were detected in the sulfite reductase reaction catalyzed by a cell-free extract of photoautotrophically grown Chromatium vinosum. Hydrogen was consumed upon addition of sulfite to the extract in the presence of hydrogenase and methylviologen. Hydrogen uptake proceeded biphasically. During the first phase, thiosulfate and sulfide were formed concomitant with the decrease in sulfite. After the disappearance of sulfite, hydrogen was consumed with reduced velocity and sulfide accumulated as the final product with the total consumption of three mol of hydrogen per mol of sulfite. The molecular weight of a major sulfite reductase was estimated to be about 180,000 by the polyacrylamide disc electrophoresis method using enzyme staining. Arsenite. EDTA, alpha,alpha'-dipyridyl, cyanide, or azide did not inhibit the activity at the concentration of 1 mM. The activity was present in the soluble fraction and was stable at --20 degrees C.
在光合自养生长的嗜硫色杆菌无细胞提取物催化的亚硫酸盐还原酶反应中检测到了硫代硫酸盐和硫化物。在有氢化酶和甲基紫精存在的情况下,向提取物中添加亚硫酸盐时会消耗氢气。氢气的摄取呈双相进行。在第一阶段,随着亚硫酸盐的减少,硫代硫酸盐和硫化物同时形成。亚硫酸盐消失后,氢气以降低的速度被消耗,硫化物作为最终产物积累,每摩尔亚硫酸盐消耗三摩尔氢气。通过使用酶染色的聚丙烯酰胺圆盘电泳法估计,一种主要的亚硫酸盐还原酶的分子量约为180,000。亚砷酸盐、乙二胺四乙酸(EDTA)、α,α'-联吡啶、氰化物或叠氮化物在1 mM浓度下不抑制该活性。该活性存在于可溶性部分中,并且在-20℃下稳定。