Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1777, Issue 9, Pages 1211-1217Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2008.05.002
Keywords
cytochrome cz; cytochrome c-554; green sulfur bacteria; menaquinol : cytochrome c oxidoreductase; reaction center; sulfur oxidation
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Funding
- Osaka University
- Ministry of Education, Culture, Sports, Science, and Technology of Japan [19614008, 19370064]
- Japan Society for the Promotion of Science [181481]
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We studied the regulation mechanism of electron donations from menaquinol:cytochrome c oxidoreductase and cytochrome c-554 to the type I homodimeric photosynthetic reaction center complex of the green sulfur bacterium Chlorobium tepidum. We measured flash-induced absorption changes of multiple cytochromes in the membranes prepared from a mutant devoid of cytochrome c-554 or in the reconstituted membranes by exogenously adding cytochrome c-555 purified from Chlorobium limicola. The results indicated that the photo-oxidized cytochrome c, bound to the reaction center was rereduced rapidly by cytochrome c-555 as well as by the menaquinol:cytochrome c oxidoreductase and that cytochrome c-555 did not function as a shuttle-like electron carrier between the menaquinol:cytochrome c oxidoreductase and cytochrome c(z) It was also shown that the rereduction rate of cytochrome c(z) by cytochrome c-555 was as high as that by the menaquinol:cytochrome c oxidoreductase. The two electron-transfer pathways linked to sulfur metabolisms seem to function independently to donate electrons to the reaction center. (C) 2008 Elsevier B.V. All rights reserved.
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