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Journal of Bacteriology, March 2001, p. 2013-2024, Vol. 183, No. 6
Department of Biology, Plant Science
Institute, University of Pennsylvania, Philadelphia, Pennsylvania
191041; Marmara Research Center,
Research Institute for Genetic Engineering and Biotechnology, Gebze,
Kocaeli 41470, Turkey2; and
Department of Biology, University of Bologna, Bologna 40126, Italy3
Received 25 September 2000/Accepted 31 October 2000
We have recently established that the facultative phototrophic
bacterium Rhodobacter sphaeroides, like the closely related Rhodobacter capsulatus species, contains both the
previously characterized mobile electron carrier cytochrome
c2 (cyt c2) and the
more recently discovered membrane-anchored cyt
cy. However, R. sphaeroides cyt cy, unlike that of R. capsulatus,
is unable to function as an efficient electron carrier between the
photochemical reaction center and the cyt bc1
complex during photosynthetic growth. Nonetheless, R. sphaeroides cyt cy can act at least
in R. capsulatus as an electron carrier between the cyt
bc1 complex and the
cbb3-type cyt c oxidase
(cbb3-Cox) to support respiratory
growth. Since R. sphaeroides harbors both a
cbb3-Cox and an
aa3-type cyt c oxidase (aa3-Cox), we examined whether
R. sphaeroides cyt cy can act
as an electron carrier to either or both of these respiratory terminal oxidases. R. sphaeroides mutants which lacked either
cyt c2 or cyt cy and
either the aa3-Cox or the
cbb3-Cox were obtained. These double mutants contained linear respiratory electron transport pathways
between the cyt bc1 complex and the cyt
c oxidases. They were characterized with respect to growth
phenotypes, contents of a-, b-, and
c-type cytochromes, cyt c oxidase activities,
and kinetics of electron transfer mediated by cyt
c2 or cyt cy. The findings demonstrated that both cyt c2 and cyt
cy are able to carry electrons efficiently from
the cyt bc1 complex to either the
cbb3-Cox or the
aa3-Cox. Thus, no dedicated
electron carrier for either of the cyt c oxidases is
present in R. sphaeroides. However, under semiaerobic
growth conditions, a larger portion of the electron flow out of the cyt
bc1 complex appears to be mediated via the cyt
c2-to-cbb3-Cox
and cyt
cy-to-cbb3-Cox
subbranches. The presence of multiple electron carriers and cyt
c oxidases with different properties that can operate
concurrently reveals that the respiratory electron transport pathways
of R. sphaeroides are more complex than those of
R. capsulatus.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.6.2013-2024.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Mobile Cytochrome c2 and Membrane-Anchored
Cytochrome cy Are Both Efficient Electron Donors
to the cbb3- and
aa3-Type Cytochrome c
Oxidases during Respiratory Growth of Rhodobacter
sphaeroides

*
Corresponding author. Mailing address: Department of
Biology, Plant Science Institute, University of Pennsylvania,
Philadelphia, PA 19104. Phone: (215) 898-4394. Fax: (215) 989-8780. E-mail: fdaldal{at}sas.upenn.edu.
Present address: Institut de Génétique et
Microbiologie, Université Paris XI, 91405 Orsay Cedex, France.
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