Grombein S, Rüdiger W, Zimmermann H
Hoppe Seylers Z Physiol Chem. 1975 Nov;356(11):1709-14. doi: 10.1515/bchm2.1975.356.2.1709.
Spectral measurements of phytochrome are performed after unfolding of the peptide chain. By comparison with bile pigments of known structure, structure 1a, containing a hydrogenated ring A, is deduced for the PR chromophore. Its spectral properties indicate that the chromophore of the physiologically active PFR form has lost the double bond of the bridge joining rings A and B.
在肽链展开后进行植物色素的光谱测量。通过与已知结构的胆汁色素比较，推断出PR发色团具有结构1a，其中含有一个氢化的A环。其光谱特性表明，生理活性PFR形式的发色团已失去连接A环和B环的桥的双键。
