Cytochrome c' (Cyt c') is a c-type cytochrome with a pentacoordinate heme iron. The gene encoding this protein in Rhodobacter sphaeroides 2.4.3, designated cycP, was isolated and sequenced. Northern blot analysis and beta-galactosidase assays demonstrated that cycP transcription increased as oxygen levels decreased and was not repressed under denitrifying conditions as observed in another Rhodobacter species. CO difference spectra performed with extracts of cells grown under different conditions revealed that Cyt c' levels were highest during photosynthetic denitrifying growth conditions. The increase in Cyt c' under this condition was higher than would be predicted from transcriptional studies. Electron paramagnetic resonance analysis of whole cells demonstrated that Cyt c' binds NO during denitrification. Mass spectrometric analysis of nitrogen oxides produced by cells and purified protein did not indicate that Cyt c' has NO reductase activity. Taken together, these results suggest a model where Cyt c' in R. sphaeroides 2.4.3 may shuttle NO to the membrane, where it can be reduced.
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http://dx.doi.org/10.1128/JB.187.12.4077-4085.2005 | DOI Listing |
Chemosphere
March 2020
Microbiology and Metabolic Engineering of Key Laboratory of Sichuan Province, College of Life Sciences, Sichuan University, Chengdu, 610064, China. Electronic address:
Microorganisms and microbial products can be highly efficient in uptaking soluble and particulate forms of heavy metals, particularly from solutions. In this study, the removal efficiency, oxidative damage, antioxidant system, and the possible removal mechanisms were investigated in Rhodobacter (R.) sphaeroides SC01 under mercury (Hg), lead (Pb) and cadmium (Cd) stress.
View Article and Find Full Text PDFMol Microbiol
December 2018
Department of Biological Sciences, Bowling Green State University, Bowling Green, OH, USA.
Strains of the phototrophic alpha-proteobacterium Rhodobacter sphaeroides vary in the number of enzymes catalyzing the formation of 5-aminolevulinic acid (ALA synthases) that are encoded in their genomes. All have hemA, but not all have hemT. This study compared transcription of these genes, and also properties of their products among three wild-type strains; 2.
View Article and Find Full Text PDFPhotosynth Res
June 2016
Laboratoire Mécanismes Fondamentaux de la Bioénergétique, UMR 8221, CEA - iBiTec-S, CNRS, Université Paris Sud, 91191, Gif-Sur-Yvette, France.
In contrast with findings on the wild-type Rhodobacter sphaeroides reaction center, biexponential P (+) H A (-) → PH A charge recombination is shown to be weakly dependent on temperature between 78 and 298 K in three variants with single amino acids exchanged in the vicinity of primary electron acceptors. These mutated reaction centers have diverse overall kinetics of charge recombination, spanning an average lifetime from ~2 to ~20 ns. Despite these differences a protein relaxation model applied previously to wild-type reaction centers was successfully used to relate the observed kinetics to the temporal evolution of the free energy level of the state P (+) H A (-) relative to P (+) B A (-) .
View Article and Find Full Text PDFJ Bacteriol
June 2014
Department of Microbiology, Cornell University, Ithaca, New York, USA
Many denitrifying organisms contain the norEF gene cluster, which codes for two proteins that are thought to be involved in denitrification because they are expressed during the reduction of nitrite and nitric oxide. The products of both genes are predicted to be membrane associated, and the norE product is a member of the cytochrome c oxidase subunit III family. However, the specific role of norEF is unknown.
View Article and Find Full Text PDFPhotosynth Res
February 2014
Division of Physics and Astronomy, Faculty of Sciences, VU University Amsterdam, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands,
In purple bacteria of the genus Rhodobacter (Rba.), an LH1 antenna complex surrounds the photochemical reaction centre (RC) with a PufX protein preventing the LH1 complex from completely encircling the RC. In membranes of Rba.
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