Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.12.7.2 (hydrogenase)
 3,522 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The carbon monoxide dehydrogenase from the photosynthetic bacterium Rhodospirillum rubrum was purified over 600-fold by DEAE-cellulose chromatography, heat treatment, hydroxylapatite chromatography, and preparative scale gel electrophoresis. In vitro, this enzyme catalyzed a two-electron oxidation of CO to form CO2 as the product. The reaction was dependent on the addition of an electron acceptor. The enzyme was oxygen labile, heat stable, and resistant to tryptic and chymotryptic digestion. Optimum in vitro activity occurred at pH 10.0. A sensitive, hemoglobin-based assay for measuring dissolved CO levels is presented. The in vitro Km for CO was determined to be 110 microM. CO, through an unknown mechanism, stimulated hydrogen evolution in whole cells, suggesting the presence of a reversible hydrogenase in R. rubrum which is CO insensitive in vivo.
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PMID:Carbon monoxide dehydrogenase from Rhodospirillum rubrum. 643 Aug 75

Early metabolic changes have been studied in the peripheral blood, brain, adrenals, spleen, and liver of rats after irradiation with 500 Gy. Using ESR spectroscopy we showed the formation of a great amount of hemoglobin nitrosyl complexes and methemoglobin in the blood and spleen, thus suggesting that the endothelium-derived relaxing factor, nitric oxide (NO), was released due to irradiation stimulation and sharp hypoxia in brain. Polarographic data concerning the disturbance of brain mitochondrial function (activation of succinate hydrogenase oxidation) allowed a conclusion that hypoxia appeared after irradiation at superlethal doses. Antioxidative activity of lipids in various tissues differed in the rats with "the early loss of performance" syndrome and in normal rats. Possibility of ammonia intoxication of the brain soon after irradiation at superlethal doses has been discussed.
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PMID:[Rapid metabolic changes in the blood and organs of rats under the influence of electron pulse radiation at superhigh doses]. 818 40

Since proteins are dynamic systems in living organisms, the employment of methodologies contemplating this crucial characteristic results fundamental to allow revealing several aspects of their function. In this work, we present results obtained using classical mechanical atomistic simulation tools applied to understand the connection between protein dynamics and ligand migration. Firstly, we will present a review of the different sampling schemes used in the last years to obtain both ligand migration pathways and the thermodynamic information associated with the process. Secondly, we will focus on representative examples in which the schemes previously presented are employed, concerning the following: i) ligand migration, tunnels, and cavities in myoglobin and neuroglobin; ii) ligand migration in truncated hemoglobin members; iii) NO escape and conformational changes in nitrophorins; iv) ligand selectivity in catalase and hydrogenase; and v) larger ligand migration: the P450 and haloalkane dehalogenase cases. This article is part of a Special Issue entitled: Protein Dynamics: Experimental and Computational Approaches.
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PMID:Protein dynamics and ligand migration interplay as studied by computer simulation. 2079 53