Rhodobacter capsulatus
Rhodobacter
Cytochromes c2
Methylococcus capsulatus
Rhodopseudomonas
Photosynthetic Reaction Center Complex Proteins
Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II.
Photosynthesis
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)
Nitrogenase
Molybdenum
Gene Expression Regulation, Bacterial
Rhodospirillaceae
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Light-Harvesting Protein Complexes
Bacterial Chromatophores
Operon
Oxidoreductases
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Electron Transport Complex III
A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.
Amino Acid Sequence
Cytochrome c Group
Tetrapyrroles
Methylococcaceae
Aerobiosis
Life or metabolic reactions occurring in an environment containing oxygen.
Cytochromes c1
The 30-kDa membrane-bound c-type cytochrome protein of mitochondria that functions as an electron donor to CYTOCHROME C GROUP in the mitochondrial and bacterial RESPIRATORY CHAIN. (From Enzyme Nomenclature, 1992, p545)
Nitrogen Fixation
Iron-Sulfur Proteins
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
Base Sequence
Electron Transport
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
Oxidation-Reduction
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
Hydrogenase
An enzyme found in bacteria. It catalyzes the reduction of FERREDOXIN and other substances in the presence of molecular hydrogen and is involved in the electron transport of bacterial photosynthesis.
Anaerobiosis
The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Ferredoxins
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Xanthine Dehydrogenase
PII Nitrogen Regulatory Proteins
Carotenoids
Genetic Complementation Test
Cosmids
Restriction Mapping
Phototrophic Processes
Processes by which phototrophic organisms use sunlight as their primary energy source. Contrasts with chemotrophic processes which do not depend on light and function in deriving energy from exogenous chemical sources. Photoautotrophy (or photolithotrophy) is the ability to use sunlight as energy to fix inorganic nutrients to be used for other organic requirements. Photoautotrophs include all GREEN PLANTS; GREEN ALGAE; CYANOBACTERIA; and green and PURPLE SULFUR BACTERIA. Photoheterotrophs or photoorganotrophs require a supply of organic nutrients for their organic requirements but use sunlight as their primary energy source; examples include certain PURPLE NONSULFUR BACTERIA. Depending on environmental conditions some organisms can switch between different nutritional modes (AUTOTROPHY; HETEROTROPHY; chemotrophy; or phototrophy) to utilize different sources to meet their nutrients and energy requirements.
Cloning, Molecular
Tellurium
Spectrophotometry
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Rhodobacter sphaeroides
Spherical phototrophic bacteria found in mud and stagnant water exposed to light.
Mutation
Escherichia coli
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
Pteridines
Flavodoxin
Coenzymes
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
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.
Acetylene
Acetylene is not typically considered a medical term, but rather a chemical compound (C2H2) commonly used in industrial and laboratory settings for its high energy content and reactivity, which may have various applications in medicine such as wound healing and surgical procedures, but it is not a medical diagnosis or disease.
Bacterial Proton-Translocating ATPases
Membrane-bound proton-translocating ATPases that serve two important physiological functions in bacteria. One function is to generate ADENOSINE TRIPHOSPHATE by utilizing the energy provided by an electrochemical gradient of protons across the cellular membrane. A second function is to counteract a loss of the transmembrane ion gradient by pumping protons at the expense of adenosine triphosphate hydrolysis.
Sequence Homology, Amino Acid
Oxidoreductases Acting on CH-CH Group Donors
Neutral Red
2,4-Dinitrophenol
Metalloproteins
Plasmids
Electron Transport Complex IV
A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.
Hydrogen
The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.
Oxygen
Spectrum Analysis
Proton-Motive Force
Energy that is generated by the transfer of protons or electrons across an energy-transducing membrane and that can be used for chemical, osmotic, or mechanical work. Proton-motive force can be generated by a variety of phenomena including the operation of an electron transport chain, illumination of a PURPLE MEMBRANE, and the hydrolysis of ATP by a proton ATPase. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p171)
Xanthobacter
A genus of gram-negative, aerobic, rod-shaped bacteria found in wet soil containing decaying organic material and in water. Cells tend to be pleomorphic if grown on media containing succinate or coccoid if grown in the presence of an alcohol as the sole carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Heme
Open Reading Frames
Sequence Analysis, DNA
Flavoproteins
Protoporphyrins
Mutagenesis, Insertional
Mutagenesis where the mutation is caused by the introduction of foreign DNA sequences into a gene or extragenic sequence. This may occur spontaneously in vivo or be experimentally induced in vivo or in vitro. Proviral DNA insertions into or adjacent to a cellular proto-oncogene can interrupt GENETIC TRANSLATION of the coding sequences or interfere with recognition of regulatory elements and cause unregulated expression of the proto-oncogene resulting in tumor formation.