Abstract
When bound to water-soluble proteins of the WSCP family, chlorophyll molecules form dimers structurally similar to “special pair” of chlorophylls (bacteriochlorophylls) in photosynthetic reaction centers. Being exposed to red light (λ ≥ 650 nm) in oxygen-free solutions, chlorophyll a dimers harbored by BoWSCP holoproteins (from Brassica oleracea var. botrytis) have sensitized the reduction of cytochrome c. According to absorption and circular dichroism spectroscopy data, the photochemical process did not significantly impair the structure of chlorophyll a molecules as well as their dimers harbored by BoWSCP protein. Adding tris(hydroxymethyl)aminomethane as an electron donor for chlorophyll recovery stimulated the photoreduction of cytochrome c.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
