Results 111 to 120 of about 7,987 (160)
Integration of NO and H<sub>2</sub>S signaling in higher plants. [PDF]
Plant CommunCorpas FJ, Taboada J, Palma JM.
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Studies on yeast sulfite reductase
BBA - Proteins and Proteomics, 1982Akio Yoshimoto
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Sulfite Reductase of Escherichia coli Is a Ferrisiderophore Reductase
Biochemical and Biophysical Research Communications, 1993A soluble ferrisiderophore reductase activity of Escherichia coli was purified to homogeneity and identified as the sulfite reductase. The pure enzyme catalyzes the reduction of ferric citrate, ferriaerobactin, ferrioxamin, ferricrocin, ferrichrome and ferrifusarinin by NADPH. Free flavins, riboflavin, FMN, FAD were absolutely required, suggesting that
J, Coves, M, Eschenbrenner, M, Fontecave
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Domain crossover in the reductase subunit of NADPH-dependent assimilatory sulfite reductase
Journal of Structural Biology, 2023NADPH-dependent assimilatory sulfite reductase (SiR) from Escherichia coli performs a six-electron reduction of sulfite to the bioavailable sulfide. SiR is composed of a flavoprotein (SiRFP) reductase subunit and a hemoprotein (SiRHP) oxidase subunit. There is no known high-resolution structure of SiR or SiRFP, thus we do not yet fully understand how ...
Nidhi Walia +6 more
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Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1968
Abstract Enzymes catalyzing the reduction of sulfite by reduced methyl viologen (MVH) were partially purified from four mutants of Saccharomyces cerevisiae, strains 6, 11, 20 and 21, which are genetically blocked in the sulfite reduction step in the sulfate assimilation pathway.
A, Yoshimoto, R, Sato
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Abstract Enzymes catalyzing the reduction of sulfite by reduced methyl viologen (MVH) were partially purified from four mutants of Saccharomyces cerevisiae, strains 6, 11, 20 and 21, which are genetically blocked in the sulfite reduction step in the sulfate assimilation pathway.
A, Yoshimoto, R, Sato
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The NADPH: Sulfite Reductase of Escherichia coli is a Paraquat Reductase
European Journal of Biochemistry, 1994The NADPH:sulfite reductase of Escherichia coli is a soluble enzyme that has a subunit structure α8β4, where the α subunit is a flavoprotein and the β subunit is a metalloprotein. Overexpression of the holoenzyme in E. coli has greatly simplified the purification of this enzyme.
P, Gaudu, M, Fontecave
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Domain Evolution and Functional Diversification of Sulfite Reductases
Astrobiology, 2005Sulfite reductases are key enzymes of assimilatory and dissimilatory sulfur metabolism, which occur in diverse bacterial and archaeal lineages. They share a highly conserved domain "C-X5-C-n-C-X3-C" for binding siroheme and iron-sulfur clusters that facilitate electron transfer to the substrate.
Ashita, Dhillon +4 more
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The relationship between structure and function for the sulfite reductases
Current Opinion in Structural Biology, 1996The six-electron reductions of sulfite to sulfide and nitrite to ammonia, fundamental to early and contemporary life, are catalyzed by diverse sulfite and nitrite reductases that share an unusual prosthetic assembly in their active centers, namely siroheme covalently linked to an Fe4S4 cluster.
B R, Crane, E D, Getzoff
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Molecular BioSystems, 2012
Abstract Rhodococcus erythropolis has been widely studied for desulfurization. However, activity levels required for commercial application have not been achieved. A major limitation of the current work in biodesulfurization is inadequate information regarding sulfur metabolism generally, and in particular the metabolism of the sulfur
Aggarwal, S. +3 more
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Abstract Rhodococcus erythropolis has been widely studied for desulfurization. However, activity levels required for commercial application have not been achieved. A major limitation of the current work in biodesulfurization is inadequate information regarding sulfur metabolism generally, and in particular the metabolism of the sulfur
Aggarwal, S. +3 more
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The third subunit of desulfoviridin‐type dissimilatory sulfite reductases
European Journal of Biochemistry, 1992In addition to the 50‐kDa (α) and 40‐kDa (β) subunits, an 11‐kDa polypeptide has been discovered in highly purified Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase. This is in contrast with the hitherto generally accepted α2β2 tetrameric subunit composition. Purification, high‐ionic‐strength gel‐filtration, native electrophoresis
Pierik, A.J. +4 more
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