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The Biological Bulletin Jun 1949
Topics: Hormones; Oxidation-Reduction
PubMed: 18153116
DOI: No ID Found -
Physiological Zoology Apr 1951
Topics: Animals; Cnidaria; Oxidation-Reduction
PubMed: 14843833
DOI: 10.1086/physzool.24.2.30163256 -
The Journal of Biological Chemistry Dec 1949
Topics: Disulfides; Oxidation-Reduction; Sulfhydryl Compounds
PubMed: 15393780
DOI: No ID Found -
Oxidative Medicine and Cellular... 2012
Topics: Cells; Diet; Disease; Oxidation-Reduction; Polyphenols
PubMed: 23213346
DOI: 10.1155/2012/583901 -
Science (New York, N.Y.) Apr 2016The splitting of dinitrogen (N2) and reduction to ammonia (NH3) is a kinetically complex and energetically challenging multistep reaction. In the Haber-Bosch process, N2...
The splitting of dinitrogen (N2) and reduction to ammonia (NH3) is a kinetically complex and energetically challenging multistep reaction. In the Haber-Bosch process, N2 reduction is accomplished at high temperature and pressure, whereas N2 fixation by the enzyme nitrogenase occurs under ambient conditions using chemical energy from adenosine 5'-triphosphate (ATP) hydrolysis. We show that cadmium sulfide (CdS) nanocrystals can be used to photosensitize the nitrogenase molybdenum-iron (MoFe) protein, where light harvesting replaces ATP hydrolysis to drive the enzymatic reduction of N2 into NH3 The turnover rate was 75 per minute, 63% of the ATP-coupled reaction rate for the nitrogenase complex under optimal conditions. Inhibitors of nitrogenase (i.e., acetylene, carbon monoxide, and dihydrogen) suppressed N2 reduction. The CdS:MoFe protein biohybrids provide a photochemical model for achieving light-driven N2 reduction to NH3.
Topics: Adenosine Triphosphate; Ammonia; Cadmium Compounds; Catalysis; Hydrolysis; Light; Molybdoferredoxin; Nanoparticles; Nitrogen; Nitrogen Fixation; Nitrogenase; Oxidation-Reduction; Sulfides
PubMed: 27102481
DOI: 10.1126/science.aaf2091 -
Journal of Bacteriology Nov 1955
Topics: Hydrogenase; Methylene Blue; Oxidation-Reduction; Oxidoreductases
PubMed: 13271299
DOI: 10.1128/jb.70.5.608-613.1955 -
The Journal of Experimental Zoology Mar 1947
Topics: Animals; Hydra; Oxidation-Reduction
PubMed: 20290997
DOI: 10.1002/jez.1401040202 -
International Journal of Molecular... Aug 2015Photodynamic therapy (PDT) is a clinical modality used to treat cancer and infectious diseases. The main agent is the photosensitizer (PS), which is excited by light and... (Review)
Review
Photodynamic therapy (PDT) is a clinical modality used to treat cancer and infectious diseases. The main agent is the photosensitizer (PS), which is excited by light and converted to a triplet excited state. This latter species leads to the formation of singlet oxygen and radicals that oxidize biomolecules. The main motivation for this review is to suggest alternatives for achieving high-efficiency PDT protocols, by taking advantage of knowledge on the chemical and biological processes taking place during and after photosensitization. We defend that in order to obtain specific mechanisms of cell death and maximize PDT efficiency, PSes should oxidize specific molecular targets. We consider the role of subcellular localization, how PS photochemistry and photophysics can change according to its nanoenvironment, and how can all these trigger specific cell death mechanisms. We propose that in order to develop PSes that will cause a breakthrough enhancement in the efficiency of PDT, researchers should first consider tissue and intracellular localization, instead of trying to maximize singlet oxygen quantum yields in in vitro tests. In addition to this, we also indicate many open questions and challenges remaining in this field, hoping to encourage future research.
Topics: Animals; Cell Death; Humans; Oxidation-Reduction; Photochemistry; Photochemotherapy; Photosensitizing Agents
PubMed: 26334268
DOI: 10.3390/ijms160920523 -
Annual Review of Biochemistry 1946
Topics: Oxidation-Reduction
PubMed: 20995962
DOI: 10.1146/annurev.bi.15.070146.000245 -
Archives Internationales de... Feb 1963
Topics: Blood; Humans; Methylene Blue; Oxidation-Reduction
PubMed: 14003608
DOI: No ID Found