Nov 1, 1975

The structures of the phytochrome chromophore in both photoreversible forms

Hoppe-Seyler's Zeitschrift für physiologische Chemie
S GrombeinH Zimmermann

Abstract

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.

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Mentioned in this Paper

Plasma Protein Binding Capacity
Protein Conformation
Bile Pigments
Spectrophotometry
Bilin
Guanidines
Protein Denaturation
Phytochrome
Hydrogen-Ion Concentration
Plant Proteins

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