Protein Information

ID 454
Name cytochrome b
Synonyms COB; CYTB; Cytochrome b; Cytochrome b of complex III; MT CYB; MTCYB; mitochondrially encoded cytochrome b; Cytochrome bs…

Compound Information

ID 309
Name sulfur
CAS sulfur

Reference

PubMed Abstract RScore(About this table)
19861232 Sang M, Ma F, Xie J, Chen XB, Wang KB, Qin XC, Wang WD, Zhao JQ, Li LB, Zhang JP, Kuang TY: High-light induced singlet oxygen formation in cytochrome b (6) f complex from Bryopsis corticulans as detected by EPR spectroscopy. Biophys Chem. 2010 Jan;146(1):7-12. Epub 2009 Oct 6.
Electron paramagnetic resonance (EPR) spectroscopy was used to detect the light-induced formation of singlet oxygen ((1) O (2)*) in the intact and the Rieske-depleted cytochrome b (6) f complexes (Cyt b (6) f) from Bryopsis corticulans, as well as in the isolated Rieske Fe-S protein. It is shown that, under white-light illumination and aerobic conditions, chlorophyll a (Chl a) bound in the intact Cyt b (6) f can be bleached by light-induced (1) O (2)*, and that the (1) O (2)* production can be promoted by D (2) O or scavenged by extraneous antioxidants such as l-histidine, ascorbate, beta-carotene and glutathione. Under similar experimental conditions, (1) O (2)* was also detected in the Rieske-depleted Cyt b (6) f complex, but not in the isolated Rieske Fe-S protein. The results prove that Chl a cofactor, rather than Rieske Fe-S protein, is the specific site of (1) O (2)* formation, a conclusion which draws further support from the generation of (1) O (2)* with selective excitation of Chl a using monocolor red light.
2(0,0,0,2)