Department of Biological Sciences Lilly Hall of Life Sciences, Purdue University, 47907, West Lafayette, Indiana, (U.S.A.).
Photosynth Res. 1986 Jan;10(3):393-403. doi: 10.1007/BF00118305.
A sumary of biochemical, biophysical, and molecular biological data is presented which led to the identification of two different polypeptides (α and β, MW=9.16 and 4.27 kDa) in the cytochrome b-559 protein. The presence of a single His residue on each polypeptide, and the conclusion from spectroscopy that the heme coordination must be bis-histidine led to an obligatory requirement for coordination of a single heme through a heme cross-linked dimer. This structure does not have a precedent among soluble or membrane bound cytochromes. The possible participation of the cytochrome in the pathway of photoactivation is discussed.
本文总结了生物化学、生物物理学和分子生物学方面的数据，由此鉴定出细胞色素 b-559 蛋白中有两种不同的多肽（α和β，MW=9.16 和 4.27 kDa）。每个多肽上只有一个组氨酸残基，从光谱学得出的结论是血红素的配位必须是双组氨酸，这就必须通过血红素交联二聚体来配位单个血红素。这种结构在可溶性或膜结合细胞色素中没有先例。本文还讨论了细胞色素参与光激活途径的可能性。
