BIOMAT Database Logo BIOMAT Database Logo

The effect of detergents and lipids on the properties of the outer-membrane protein OmcA from Shewanella oneidensis. 2010

Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Department of Biophysics, Medical College of Wisconsin, Milwaukee, USA.

The protein OmcA from the bacterium Shewanella oneidensis was purified to homogeneity, and characterized using UV-vis spectroelectrochemistry, EPR, and circular dichroism (far- and near-UV regions). EPR spectroscopy showed that many different c-type hemes are present in the protein: high-spin, low-spin, and highly anisotropic low-spin hemes were all detected. The protein was shown to bind tightly to artificial membranes (liposomes) composed of dioleoylphosphatidylglycerol and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (60:40 molar ratio), which mimic the natural environment. However, on the basis of the spectroscopic and electrochemical studies, binding to liposomes does not appear to significantly alter either the structure or the properties of OmcA. On the other hand, the electrochemical properties of OmcA are noticeably changed in the presence of the detergents used during the initial purification stages. In particular, the reduction potentials of two out of the ten OmcA hemes appear to shift in the presence of detergent, perhaps because these hemes are solvent-exposed.

UI MeSH Term Description Entries
D008081 Liposomes Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins. Niosomes,Transferosomes,Ultradeformable Liposomes,Liposomes, Ultra-deformable,Liposome,Liposome, Ultra-deformable,Liposome, Ultradeformable,Liposomes, Ultra deformable,Liposomes, Ultradeformable,Niosome,Transferosome,Ultra-deformable Liposome,Ultra-deformable Liposomes,Ultradeformable Liposome
D003902 Detergents Purifying or cleansing agents, usually salts of long-chain aliphatic bases or acids, that exert cleansing (oil-dissolving) and antimicrobial effects through a surface action that depends on possessing both hydrophilic and hydrophobic properties. Cleansing Agents,Detergent Pods,Laundry Detergent Pods,Laundry Pods,Syndet,Synthetic Detergent,Agent, Cleansing,Agents, Cleansing,Cleansing Agent,Detergent,Detergent Pod,Detergent Pod, Laundry,Detergent Pods, Laundry,Detergent, Synthetic,Detergents, Synthetic,Laundry Detergent Pod,Laundry Pod,Pod, Detergent,Pod, Laundry,Pod, Laundry Detergent,Pods, Detergent,Pods, Laundry,Pods, Laundry Detergent,Synthetic Detergents
D004563 Electrochemistry The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes. Electrochemistries
D004578 Electron Spin Resonance Spectroscopy A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING. ENDOR,Electron Nuclear Double Resonance,Electron Paramagnetic Resonance,Paramagnetic Resonance,Electron Spin Resonance,Paramagnetic Resonance, Electron,Resonance, Electron Paramagnetic,Resonance, Electron Spin,Resonance, Paramagnetic
D001425 Bacterial Outer Membrane Proteins Proteins isolated from the outer membrane of Gram-negative bacteria. OMP Proteins,Outer Membrane Proteins, Bacterial,Outer Membrane Lipoproteins, Bacterial
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013056 Spectrophotometry, Ultraviolet Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Ultraviolet Spectrophotometry
D020592 Shewanella A genus of gram-negative, facultatively anaerobic rods. It is a saprophytic, marine organism which is often isolated from spoiling fish.

Related Publications

Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Crystallization and preliminary X-ray crystallographic studies of the outer membrane cytochrome OmcA from Shewanella oneidensis MR-1.
January 2012, Acta crystallographica. Section F, Structural biology and crystallization communications,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Electrical properties of outer membrane extensions from Shewanella oneidensis MR-1.
November 2021, Nanoscale,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
The Outer Membrane Cytochrome OmcA Is Essential for Infection of Shewanella oneidensis by a Zebrafish-Associated Bacteriophage.
June 2023, Journal of bacteriology,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Specific bonds between an iron oxide surface and outer membrane cytochromes MtrC and OmcA from Shewanella oneidensis MR-1.
July 2007, Journal of bacteriology,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Role of outer-membrane cytochromes MtrC and OmcA in the biomineralization of ferrihydrite by Shewanella oneidensis MR-1.
January 2010, Geobiology,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Transcriptional mechanisms for differential expression of outer membrane cytochrome genes omcA and mtrC in Shewanella oneidensis MR-1.
March 2015, BMC microbiology,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Kinetics of reduction of Fe(III) complexes by outer membrane cytochromes MtrC and OmcA of Shewanella oneidensis MR-1.
November 2008, Applied and environmental microbiology,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Direct involvement of type II secretion system in extracellular translocation of Shewanella oneidensis outer membrane cytochromes MtrC and OmcA.
August 2008, Journal of bacteriology,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Antibody recognition force microscopy shows that outer membrane cytochromes OmcA and MtrC are expressed on the exterior surface of Shewanella oneidensis MR-1.
May 2009, Applied and environmental microbiology,
Gregory J Bodemer, and William A Antholine, and Liana V Basova, and Daad Saffarini, and A Andrew Pacheco
Isolation of a high-affinity functional protein complex between OmcA and MtrC: Two outer membrane decaheme c-type cytochromes of Shewanella oneidensis MR-1.
July 2006, Journal of bacteriology,
Copied contents to your clipboard!