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- 3Electron paramagnetic resonance
- 2Nitrate reductase
- 2Quinone binding site
- 1Acidithiobacillus ferrooxidans
- 1Bacterial respiratory diversity
Results for "supervisors_tesim:"Weiner, Joel (Biochemistry)""
Approximately one third of the E. coli and human proteomes consist of membrane proteins. Among these proteins are oxidoreductases, which fulfil central roles in the bioenergetic processes of cells, function as pathogenicity factors in microorganisms and their dysfunction is responsible for many...
Pyranopterin Coordination Controls Molybdenum Electrochemistry in Escherichia coli Nitrate ReductaseDownload
Molybdenum is an essential trace element for most species on the earth. Molybdoenzymes (enzymes containing Molybdenum) play diverse roles in human health, global geochemical cycles, and bacterial metabolism. Interestingly, nitrate reductase (NarGHI) isolated from the common gut bacterium...
Complex II, or succinate dehydrogenase, is a vital component of aerobic life. Its function is critical for both the tricarboxylic acid cycle and the mitochondrial respiratory chain since it catalyzes the oxidation of succinate to fumarate, liberating two electrons that feed into the lipid-soluble...
Molybdenum is a metal present in all forms of life. Most commonly, it forms the molybdenum cofactor (Moco) in the active site of molybdoenzymes. In bacteria, dimethyl sulfoxide (DMSO) reductase is a molybdoenzyme that is part of the anaerobic respiratory chain. E. coli DMSO reductase (DmsABC)...
Characterization, Structure and Mechanism of Sulfide:quinone oxidoreductase (SQR) from Acidithiobacillus ferrooxidansDownload
A key enzyme in maintaining sulfide homeostasis is the membrane-associated flavoenzyme sulfide:quinone oxidoreductase (SQR) found in nearly all domains of life (except plants). SQR maintains a critical equilibrium between sulfide (H2S, HS- and S2-) and elemental sulfur (S0), coupling the...