Knaff D B, Malkin R
Biochim Biophys Acta. 1976 May 14;430(2):244-52. doi: 10.1016/0005-2728(76)90082-7.
The iron-sulfur proteins of the green photosynthetic bacterium Chlorobium have been characterized by oxidation-reduction potentiometry in conjunction with low-temperature electron paramagnetic resonance spectroscopy. Chlorobium ferredoxin was the only iron-sulfur protein detected in the soluble fraction; no high-potential iron-sulfur protein was observed. In addition, high-potential iron-sulfur protein was not detected in the chromatophores. Four chromatophore-bound iron-sulfur proteins were detected. One is the "Rieske" type iron-sulfur protein with a g-value of 1.90 in the reduced state; the protein has a midpoint potential of + 160 mV (pH 7.0), and this potential is pH dependent. Three g=1.94 chromatophore-bound iron-sulfur proteins were observed, with midpoint potentials of -25, -175, and about -550 mV. A possible role for the latter iron-sulfur protein in the primary photochemical reaction in Chlorobium is considered.
绿色光合细菌绿菌属的铁硫蛋白已通过氧化还原电位测定法结合低温电子顺磁共振光谱进行了表征。绿菌属铁氧化还原蛋白是在可溶部分中检测到的唯一铁硫蛋白；未观察到高电位铁硫蛋白。此外，在载色体中未检测到高电位铁硫蛋白。检测到四种与载色体结合的铁硫蛋白。一种是“里斯克”型铁硫蛋白，还原态时g值为1.90；该蛋白的中点电位为 +160 mV（pH 7.0），且此电位依赖于pH。观察到三种g = 1.94的与载色体结合的铁硫蛋白，中点电位分别为 -25、-175和约 -550 mV。考虑了后一种铁硫蛋白在绿菌属初级光化学反应中的可能作用。
