Bamford V A, Berks B C, Hemmings A M
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
Biochem Soc Trans. 2002 Aug;30(4):638-42. doi: 10.1042/bst0300638.
A key component of the oxidative biogeochemical sulphur cycle involves the utilization by bacteria of reduced inorganic sulphur compounds as electron donors to photosynthetic or respiratory electron transport chains. The SoxAX protein of the photosynthetic bacterium Rhodovulum sulfidophilum is a heterodimeric c-type cytochrome that is involved in the oxidation of thiosulphate and sulphide. The recently solved crystal structure of the SoxAX complex represents the first structurally characterized example of a productive electron transfer complex between haemoproteins where both partners adopt the c-type cytochrome fold. The packing of c-type cytochrome domains both within SoxA and at the interface between the subunits of the complex has been compared with other examples and found to be unique.
氧化生物地球化学硫循环的一个关键组成部分涉及细菌利用还原态无机硫化合物作为光合或呼吸电子传递链的电子供体。嗜硫红假单胞菌的SoxAX蛋白是一种异源二聚体c型细胞色素，参与硫代硫酸盐和硫化物的氧化。最近解析的SoxAX复合物晶体结构代表了血红素蛋白之间产生性电子转移复合物的首个结构表征实例，其中两个伙伴均采用c型细胞色素折叠。已将SoxA内以及复合物亚基之间界面处的c型细胞色素结构域的堆积与其他实例进行比较，发现其具有独特性。
