The membrane-bound cytochrome cy of Rhodobacter capsulatus can serve as an electron donor to the photosynthetic reaction center of Rhodobacter sphaeroides

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Rhodobacter capsulatus has two different pathways for reduction of the photo-oxidized reaction center, one using water-soluble cytochrome c2, the other via membrane-associated cytochrome cy. Rhodobacter sphaeroides differs in that it lacks a cytochrome cy homologue capable of functioning in photosynthetic electron transfer; cytochrome c2 is thus the sole electron carrier, and is required for photosynthetic (Ps+) growth. Genetic evidence indicates that cytochrome cy of R. capsulatus can complement a Ps- cytochrome-c2-deficient mutant of R. sphaeroides (Jenney, F.E. and Daldal, F. (1993) EMBO J. 12, 1283-1292). Here, we show that it transfers electrons from the cytochrome bc1 complex to the reaction center in R. sphaeroides, albeit at a lower rate than that catalyzed by the endogenous cytochrome c2. When cytochrome cy is expressed in R. sphaeroides in the presence of cytochrome c2, there is an increase in the amount of photo-oxidizible c-type cytochrome. In the absence of cytochrome c2, electron transfer via cytochrome cy shows significantly different kinetics for reaction center reduction and cytochrome c oxidation. These findings further establish that cytochrome cy, the electron carrier permitting soluble cytochrome c2-independent photosynthetic growth in R. capsulatus, can function in a similar capacity in R. sphaeroides.

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Biochimica et Biophysica Acta - Bioenergetics



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This article was published in Biochimica et Biophysica Acta - Bioenergetics, Volume 1273, Issue 2, Pages 159-164.

The published version is available at http://dx.doi.org/10.1016/0005-2728(95)00137-9.

Copyright © 1996 Elsevier and licensed OA under an Elsevier User License.

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