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Biomedical subjects

D E Green

Publications and source records attributed to D E Green.

At least 55 records · Page 3Linked to original sources
PubMed1982

On the enzymic mechanism of oxidative phosphorylation.

Oxidative phosphorylation, like substrate-level phosphorylation, involves oxidative conversion of inorganic phosphate to a reactive species followed by interaction of this species with enzyme-bound ADP to form enzyme-bound ATP. The reactive species in a phosphoryl ester in substrate-level phosphorylation and phosphonium ion of orthophosphate in oxidative phosphorylation. The coupled synthesis is mediated by a combination of two classical enzymes in substrate-level phosphorylation and by a set of energy-coupled enzymes in oxidative phosphorylation. The full range of experimental evidence supporting this proposed enzymic mechanism of oxidative phosphorylation is presented as well as the rationalization of phenomena that hitherto have eluded explanation.

ATP Synthetase Complexes↗
PubMed1981

Cardiolipin requirement for electron transfer in complex I and III of the mitochondrial respiratory chain.

Almost complete phospholipid depletion has been achieved for Complex I and III of the mitochondrial respiratory chain using a technique that involves elution on Sephadex LH-20 in the presence of Triton X-100. Enzymic activity may be regenerated by replenishment with phospholipid. However, restoration of enzymic activity in phospholipid-depleted Complex I and III has been shown to require the presence of cardiolipin. These results are, therefore, similar to findings on the absolute catalytic requirement of cardiolipin for cytochrome oxidase activity (Fry, M., and Green, D. E. (1980) Biochem. Biophys. Res. Commun. 93, 1238-1246). At least two roles for phospholipid involvement in electron transfer processes are proposed, a catalytic role provided specifically by cardiolipin and a dispersive role that may be provided by various phospholipids or detergents. The absolute requirement of enzymic activity for cardiolipin suggests that this phospholipid plays a crucial role in the coupled electron transfer process.

Animals↗
PubMed1981

Hospital opts for "greenhouse" atmosphere in staff dining area.

The administration of St. Elizabeth Hospital, Granite City, IL, chose a staff dining area design that accents natural light, foliage, and wood finishes in an attempt to provide their employees with a relaxing, intimate place to meet.

Hospital Bed Capacity, 300 to 499↗
PubMed1981

Studies on the resolution of cytochrome oxidase.

Cytochrome oxidase has been resolved in acetic acid and high salt/detergent media. In 0.5% acetic acid, the smaller subunits of the enzyme are selectively extracted with retention of an insoluble protein fraction containing subunits I-IV, VII. This fraction retains all the heme and copper of the original enzyme in a spectrally unaltered state, and possesses enzymic activity comparable to the unresolved enzyme. The further removal of subunit IV from this fraction results in migration of heme and copper and modification of their spectral characteristics. Resolution of the enzyme in a high salt/detergent medium extracts smaller subunits (V-VII) together with subunit IV and some heme and copper. The heme associated with this enzymically active extract has spectral characteristics that are partially suggestive of heme a3. It is suggested that the fraction of subunits I-IV,VII, resolved in dilute acetic acid, may represent the limit of resolution of the cytochrome oxidase complex that remains actively and spectrally indistinguishable from the original enzyme.

Acetates↗
PubMed1981

A critique of the chemosmotic model of energy coupling.

The chemosmotic model provides a framework for visualizing energy-coupled reactions (vectorial reaction sequences, membrane-dependent gradient formation, and charge separation of reacting species) and a mechanism for energy coupling (indirect coupling between the driving and driven reaction sequences mediated by a membrane potential or a protonmotive force). The mechanistic parameters of this model have been examined from four standpoints: compatibility with the experimental realities, supporting evidence that is unambiguous, compatibility with the enzymic nature of energy coupling, and the capability for generating verifiable predictions. Recent developments that have clarified the mechanism of ion transport, the nature of the protonic changes that accompany energy coupling, and the enzymic nature of energy coupling systems have made such an examination both timely and necessary. After weighing the available evidence, it has been concluded that the chemosmotic principle of indirect coupling has no basis in fact and that it is physically unsound in respect to the mechanism of energy coupling and enzymic catalysis.

Adenosine Triphosphatases↗
PubMed1981

Universal energy principle of biological systems and the unity of bioenergetics.

Electronic energy (chemical bond energy) is the exclusive source of utilizable energy in biological systems. The release of this energy is mediated enzymically. The energy required to rupture a single covalent or ionic bond is prohibitively high under physiological conditions [in the range of 80-200 kcal/mol (1 kcal = 4.18 kJ)]. By the technique of the pairing of bond rupture (two juxtaposed bonds ruptured simultaneously) and the pairing of bond formation, enzymes can bypass the huge thermodynamic barrier to chemical change inherent in rupture of a single bond and operate within thermal limits. Enzymes accordingly can be conceived of as the energy machines that translate this principle. The principle of this transduction is that the energy required for forming a new covalent bond can fall within thermal limits when the original charged atom partner to the bond is displaced by a substitute charged atom under conditions in which the charge field of the bond remains constant during the substitution. In the transition from classical enzymology to energy coupling, muscular contraction, template-dependent replication, etc., new dimensions and possibilities are added to the basic enzymatic machinery. Specialized molecular devices (membranes, filaments, channels, templates, etc.) have to be introduced to make possible these extensions and permutations of enzymology. But it is demonstrable that the basis pairing principle is fully preserved during any of these modifications or extensions. Long range movement--of an ion, a filament, or a template--is the most important property introduced into classical enzymology in the transition to energy coupling systems.

Energy Metabolism↗
PubMed1980

Salmonellosis and arizonosis in the reptile collection at the National Zoological Park.

The prevalence of Salmonella and Arizona organisms in the reptile collection at the National Zoological Park was investigated. Culture of specimens from 311 reptiles, while live or at necropsy, yielded yielded 117 positive results, for an overall infection rate of 37%. Snakes had the highest rate, 55% (69 of 125); lizards had an intermediate rate, 36% (46 of 129); and turtles and tortoises had the lowest rate, 3% (2 of 63). Twenty-four serotypes of Salmonella enteritidis, 1 of S choleraesuis, and 39 of Arizona hinshawii were represented. While clinical illness was never directly attributed to infection with these organisms, pure cultures of Salmonella and Arizona were recovered at necropsy from some reptiles with gross and/or histologic lesions in the gastrointestinal tract, liver, spleen, and blood vessels. However, numerous other concurrent diseases and management problems were often considered the immediate cause of death, with Salmonella and Arizona being ready and significant opportunistic pathogens contributing to the demise of the reptiles.

Animals↗
PubMed1980

The localization of tightly bound cardiolipin in cytochrome oxidase.

One to two molecules of tightly bound cardiolipin are associated with resolved fractions of cytochrome oxidase containing subunits I to III or I to IV. Large scale isolation of subunits I to IV indicates the presence of approximately 0.5 molecule of cardiolipin per molecule of subunit I. Lipoprotein staining of sodium dodecyl sulfate/urea/acrylamide gels of cytochrome oxidase support the findings that subunit I is a lipoprotein. The resistance of this tightly bound cardiolipin to organic solvent extraction suggests a specific association of some tenacity with the protein.

Binding Sites↗
PubMed1980

Phospholipids as the molecular instruments of ion and solute transport in biological membranes.

Partition studies have established that phospholipids generally have the capabilities to mediate the transmembrane transport of the full range of ions and solutes that physiologically cross biological membranes. The list of transportable species includes cations, anions, amino acids, citric acid cycle intermediates, nucleotides, and sugars. Phospholipid-mediated transport can be readily modulated by altering the phospholipid mixture or by addition of detergents, nucleotides, divalent metals, proteins, peptides, or ring compounds. Containment of phospholipid within channels in protein appears to be the precondition for the formation of the micellar structure requisite for solute transport. Phospholipid-mediated transport is postulated to be a central feature of energy coupling, membrane-spanning systems, and membrane-bound, phospholipid-requiring enzymes.

Biological Transport↗