Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130-4899, USA.
Photosynth Res. 2009 Oct;102(1):43-51. doi: 10.1007/s11120-009-9482-7. Epub 2009 Aug 13.
Cytochrome c(6), (cyt c(6)) a soluble monoheme electron transport protein, was isolated and characterized from the chlorophyll d-containing cyanobacterium Acaryochoris marina, the type strain MBIC11017. The protein was purified using ammonium sulfate precipitation, ion exchange and gel filtration column chromatography, and fast performance liquid chromatography. Its molecular mass and pI have been determined to be 8.87 kDa and less than 4.2, respectively, by mass spectrometry and isoelectrofocusing (IEF). The protein has an alpha helical structure as indicated by CD (circular dichroism) spectroscopy and a reduction midpoint potential (E(m)) of +327 mV versus the normal hydrogen electrode (NHE) as determined by redox potentiometry. Its potential role in electron transfer processes is discussed.
细胞色素 c(6)（cyt c(6)）是一种可溶性单血红素电子传递蛋白，从含有叶绿素 d 的蓝藻 Acaryochoris marina 中分离和鉴定出来，其模式菌株为 MBIC11017。该蛋白使用硫酸铵沉淀、离子交换和凝胶过滤柱层析以及快速液相色谱法进行纯化。通过质谱和等电聚焦（IEF），确定其分子量和等电点分别为 8.87 kDa 和小于 4.2。CD（圆二色性）光谱表明该蛋白具有α螺旋结构，通过氧化还原电位法测定其还原中点电位（E(m)）为+327 mV 相对于标准氢电极（NHE）。讨论了其在电子传递过程中的潜在作用。
