https://microbewiki.kenyon.edu/index.

php/Rhodospirillum

Classification
Higher order taxa:
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; Rhodospirillaceae

Species:
Rhodospirillum centenum, R. photometricum, R. rubrum, R. sp.
NCBI: Taxonomy Genome

Description and Significance

Rhodospirillum rubrum is a purple nonsulfur bacterium that can grow aerobically or anaerobically. It
has the ability to live through cellular respiration, fermentation, photosynthesis, or photoautotrophic
growth.

Genome Structure
None of the genomes for bacteria in the Rhodospirillum genera have been sequenced. However,
the regulation of nitrogen fixation occurs at the transcriptional level with the nif expression and the
posttranslational level with dinitrogenase reductase by "reversible ADP-ribosylation catalyzed by the
DRAT-DRAG (dinitrogenase reductase ADP-ribosyltransferase-dinitrogenase reductase-activating
glycohydrolase) system" (Zhang et al. 1999). In addition, a genetic system of the bacterial
photosynthesis for Rhodospirillum centenum has been developed through studying mutants
(Yildiz et al. 1991). Visit the draft of the Rhodospirillum rubrum analysis files made for the Joint
Genome Institute Microbial Sequencing program for great information on the genome
of Rhodospirillum rubrum.

Cell Structure and Metabolism

Rhodospirillum bacteria are Gram-negative, motile, spiral-shaped bacteria. They can grown under
many different types of conditions including aerobic or anaerobic environments. Anaerobically, the
bacterium uses fermentation or photosynthesis in order to produce energy as well as
photoautotrophic growth (DOE). The nitrogen fixation system of R. rubrum uses a MoFe and an Feonly nitrogenase. This system, which works with both translational and post-translational regulation
of the nitrogenase activity and responds to both nitrogen and energy status signals, has been called
the "best-understood example of reversible ADP-ridosylation as a regulatory system in any
organism" (DOE).Rhodospirillum rubrum was found to be most efficient and produce the maximum
levels of internal photosynthetic membranes when it was grown with both succinate and frutose as
carbon sources under microaerophilic conditions (Grammel et al. 2003). However, it can grow with
CO as its sole energy source (DOE). The structure o fthe CODH that is the center of R. rubrum's
CO oxidation system has become a model for more complex CODHs for other organisms. In
addition, the CO-oxidation regulon has a unique CO-sensing protein, CooA, that is "becoming a
paradigm for gas-sensors and transcriptional regulators" (DOE).

In the absence of fructose, the bacterium only produced 20% of its maximum level of photosynthetic
membranes. In aerobic conditions, R. rubrum consumed the succinate and fructose simultaneously;
however, during oxygen-limiting conditions, the bacterium preferentially consumed fructose. The
cell processed the frutose through the Embden-Meyer-Parnas pathway. It was also found that
under oxygen-limiting conditions, NADPH was produced mostly by the pyridine-nucleotide
transhydrogenase. (Grammel et al. 2003)

Ecology
Rhodospirillum bacteria can generally be found in marine environments or in some types of mud
and soil where light is available for photosynthesis. Rhodospirillum centenum can form swarm
colonies that "rapidly migrate toward or away from light, depending on the wavelength of excitation"
by using surface-induced lateral flagella, chemotaxis, and a photosynthetic apparatus (Jiang et
al. 1997).

Bchl a Pathway
A genetic system of the bacterial photosynthesis in Rhodospirillum centenum was developed by
studying mutants. The mutants blocked bacteriochlorophyll a biosynthesis at certain steps of the
biosynthetic pathway leading from protoporphyrin IX to bacteriochlorophyll a. Some of the mutants
blocked carotenoid biosynthesis early in the pathway and "exhibited pleiotropic effects on stability or
assembly of the photosynthetic apparatus" (Yildiz et al. 1991). Other mutants lacked the ability to
make a functional reaction center complex; others still had defective cytochromes which resulted in
defective electron transport. The last type of mutant in this study had an "enhanced repression" of
bacteriochlorophyll due to the presence of oxygen. The genetic system and biosynthetic pathway
can be viewed in the diagram to the right.

CODH
Rhodospirillum rubrum's Ni-Fe-S carbon monoxide dehydrogenase (CODH) "catalyzes the
biological oxidation of CO at an unusual Ni-Fe-S cluster called the C-cluster" that contains a
mononuclear site and a four-metal cubane (Drennan et al. 2001). The CODH does this oxidation in
a two-electron process:

It is thought that the CO binds to a unique CO-binding site on the C-cluster adjacent to the
hydroxide; this allows a metal-bound hydroxide to "attack" the CO carbon. The metal-COOH
intermediate is then deprotonated (loses the H) and the CO 2 is "lost to yield a two-electron-reduced
C-cluster" (Drennan et al. 2001).

References
General:

DOE Joint Genome Institute:Rhodospirillum rubrum

Jiang, Ze-Yu, Brenda G. Rushing, Yong Bai, Howard Gest, and Carl E. Bauer. 1998. "Isolation
of Rhodospirillum centenum mutants defective in phototactic colony motility by transposon

mutagenesis." Journal of Bacteriology, vol. 180, no. 5. American Society for Microbiology.
(1248-1255)

Yildiz, Fitnat H., Howard Gest, and Carl E. Bauer. 1991. "Genetic analysis of photosynthesis
in Rhodospirillum centenum." Journal of Bacteriology, vol. 173, no. 13. American Society for
Microbiology. (4163-4170)

Cell Structure and Metabolism:

Grammel, Hartmut, Ernst-Deiter Gilles, and Robin Ghosh. 2003. "Microaerophilic cooperation of
reductive and oxidative pathways allows maximal photosynthetic membrane biosynthesis
in Rhodospirillum rubrum." Applied and Environmental Microbiology, vol. 69, no. 11. American
Society for Microbiology. (6577-6586)

CODH

Drennan, Catherine L., Jongyun Heo, Michael D. Sintchak, Eric Schreiter, and Paul W. Ludden.
2001. "Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon
monoxide dehydrogenase." Proceedings of the National Academy of Sciences of the USA, vol.
98, no. 21. (11973-11978)