By Stefan Weber, Erik Schleicher
In Flavins and Flavoproteins: tools and Protocols, professional researchers within the box aspect some of the equipment that are now normal to review flavins and flavoproteins. those comprise evaluate variety equipment and protocols to exemplify the diversity, the facility and the good fortune of contemporary recommendations and techniques in software to flavoproteins. half I of this quantity covers normal houses, syntheses and functions of loose flavins in addition to its analogs and flavoproteins. half II covers characterizations of flavins and flavoproteins utilizing sleek experimental ideas in addition to theoretical equipment. Written within the hugely winning Methods in Molecular Biology sequence layout, the chapters comprise the type of specific description and implementation suggestion that's the most important for buying optimum leads to the laboratory.
Thorough and intuitive, Flavins and Flavoproteins: tools and Protocols aids scientists in carrying on with to take on the numerous questions that must be replied to extra totally understand the great range and specificity of flavin-governed organic processes.
Read Online or Download Flavins and Flavoproteins: Methods and Protocols (Methods in Molecular Biology) PDF
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Extra info for Flavins and Flavoproteins: Methods and Protocols (Methods in Molecular Biology)
16a implicates the initial formation of a lumazine exomethylene anion (42), which performs a 28 Ilka Haase et al. Fig. 16 Two proposed reaction mechanisms of riboflavin synthase [73, 86] nucleophilic attack on the second substrate molecule which is then followed by ring closure under formation of the pentacyclic system 41. A more recent proposal shown in Fig. 16b also starts with the formation of the lumazine exomethylene anion (42), which subsequently donates a hydride anion to the second substrate .
Fig. 19 Biosynthesis of roseoflavin 5 A Riboflavin Synthase Paralog as Optical Transponder Certain marine bacteria use paralogs of riboflavin synthase designated lumazine protein, yellow fluorescent protein and blue fluorescent protein, respectively, as optical transponders for bioluminescence emission. The proteins are monomeric analogs of the trimeric riboflavin synthase which lack the C-terminal trimerization helix . The proteins bind 6,7-dimethyl-8-ribityllumazine, FMN, or 6-methyl-8-ribityl-2,4,7(1H,3H,8H)-pteridinetrione as chromophores which can be excited by radiationless transfer from luciferase .
107. the presence of two different flavin chromophores. Biochemistry 27:1758–1765 Glas AF, Maul MJ, Cryle M, Barends TR, Schneider S, Kaya E, Schlichting I, Carell T (2009) The archaeal cofactor F0 is a lightharvesting antenna chromophore in eukaryotes. Proc Natl Acad Sci U S A 106:11540–11545 Maul MJ, Barends TR, Glas AF, Cryle MJ, Domratcheva T, Schneider S, Schlichting I, Carell T (2008) Crystal structure and mechanism of a DNA (6-4) photolyase. Angew Chem Int Ed Engl 47:10076–10080 Mueller M, Carell T (2009) Structural biology of DNA photolyases and cryptochromes.