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, cytochrome C552
National Institutes of Health
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SERR Spectroelectrochemical Study of Cytochrome cd 1 Nitrite Reductase Co-Immobilized with Physiological Redox Partner Cytochrome c 552 on Biocompatible Metal Electrodes
Pedro O. Quintas
Corpus ID: 14197663
Cytochrome cd1 nitrite reductases (cd 1NiRs) catalyze the one-electron reduction of nitrite to nitric oxide. Due to their…
Electrochemically driven catalysis of Rhizobium sp. NT-26 arsenite oxidase with its native electron acceptor cytochrome c552.
Biochimica et biophysica acta
Corpus ID: 9037296
We describe the catalytic voltammograms of the periplasmic arsenite oxidase (Aio) from the chemolithoautotrophic bacterium…
Visible spectroelectrochemical characterization of Geobacter sulfurreducens biofilms on optically transparent indium tin oxide electrode
Corpus ID: 59042705
Abstract We report visible spectroelectrochemical (SEC) characterization of cytochrome c552 (cyt c552) in viable Geobacter…
Physiological role and redox properties of a small cytochrome c(5), cytochrome c-552, from alkaliphile, Pseudomonas alcaliphila AL15-21(T).
Journal of bioscience and bioengineering
Corpus ID: 21991952
Cytochrome c-552 from Pseudomonas alcaliphila AL15-21(T), which is a small cytochrome c(5) from Pseudomonas spp., was first…
Characterization of Peroxide‐Bound Heme Species Generated in the Reaction of Thermally Tolerant Cytochrome c552 with Hydrogen Peroxide
Chembiochem : a European journal of chemical…
Corpus ID: 22519768
Peroxide‐bound heme species have been considered difficult to detect under physiological conditions because of their…
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