Daniel V. Der Vartanian

TL;DR: A soluble hydrogenase from the methanogenic bacterium, Methanosarcina barkeri has been purified to apparent electrophoretic homogeneity, with an overall 550-fold purification, a 45% yield and a final specific activity of 270 mumol H2 evolved min-1 (mg protein)-1.

TL;DR: Publisher Summary Sulfate-reducing bacteria essentially obtain their energy for growth from the oxidation of a limited number of organic acids, ethanol, or hydogen and are used to reduce various sulfur compounds to the level of hydrogen sulfide.

TL;DR: The very high V value observed for oxidation of cytochrome d (strains AV-11 and AV-OP) suggests that this oxidase is capable of handling the electron flow generated by the very active dehydrogenases.

TL;DR: Growth rates under oxygen-excess conditions and respiratory-linked proton translocation ratios of the mutant and wild-type stains were similar as were the photochemical spectral and kinetic properties of cytochrome d.

TL;DR: The results indicate that the non-heme iron found in the purified reductase is catalytically active and that the turnover number of the enzyme-bound FAD is identical with the maximum turnover number for the enzyme.