📘 ❞ ( Reid-Flavoprotein Protocols-Humana Press (1999) ❝ كتاب ــ Stephen K. Chapman Graeme A. Reid
Biology Books - 📖 كتاب ❞ ( Reid-Flavoprotein Protocols-Humana Press (1999) ❝ ــ Stephen K. Chapman Graeme A. Reid 📖
█ _ Stephen K Chapman Graeme A Reid 0 حصريا كتاب ❞ ( Flavoprotein Protocols Humana Press (1999) ❝ 2024 (1999): نبذه عن الكتاب: The essential cofactor of flavoproteins is derived from riboflavin (Fig 1), which consists the isoalloxazine ring system with a ribityl side chain attached to central N 10 position in pyrazine moiety This precursor phosphorylated at 5' hydroxyl group by flavokinase to yield flavin mononucleotide (FMN) In second ATP dependent reaction, FAD pyrophosphorylase attaches an AMP to FMN yielding adenine dinucleotide (FAD) Both cofactors are widely distributed nature The side chain plays important role binding protein and therefore majority have strong preference for either FMN or FAD On other hand, does not play general as a cofactor flavoenzymes addition noncovalent flavin to protein, covalent linkage amino acid residue via 8 6 position of also found (see Chapter 13) all cases, the mechanistically relevant that serves as a reversible reduction oxidation catalyst many biological redox processes (for review see: (1,2)) This structural component flavin cofactor responsible light absorption UV and visible spectral range giving rise yellow appearance flavoproteins (Latin: flavus = yellow) oxidized form two peaks ≈ 360 and 450 nm observed Fig 2) Method 1 describes procedure to determine extinction coefficient bound particular flavoprotein which based on known free and FAD (12,500 11,300 M–1 cm–1, respectively) Binding to the protein alters covering range Biology Books مجاناً PDF اونلاين Biologically Biology natural science concerned study life, its various forms function, how these organisms interact each surrounding environment word biology Greek made up words: bio (βίος) meaning life And loggia λογία) means Biology: similarity vegetation animal cover edges African American states, existence same fossil Branches biology Biology ancient thousands years old modern began nineteenth century has multiple branches Among them are: Anatomy Botany Biochemia Biogeography Biofisia Cytology cell science Ecology environmental science Development Embryology embryology Genetics genetics Histology histology Anthropology anthropology Microbiology bacteriology Molecular Biology Physiology functions organs Taxonemia taxonomy Virology virology Zoology zoology
كتاب
( Reid-Flavoprotein Protocols-Humana Press (1999)
ــ Stephen K. Chapman Graeme A. Reid
كتاب
( Reid-Flavoprotein Protocols-Humana Press (1999)
ــ Stephen K. Chapman Graeme A. Reid
نبذه عن الكتاب:
The essential cofactor of flavoproteins is derived from riboflavin (Fig. 1),
which consists of the isoalloxazine ring system with a ribityl side chain attached
to the central N-10 position in the pyrazine moiety.
This precursor is phosphorylated at the 5'-hydroxyl group by flavokinase to
yield flavin mononucleotide (FMN). In a second ATP-dependent reaction, FAD
pyrophosphorylase attaches an AMP moiety to FMN yielding flavin adenine
dinucleotide (FAD). Both cofactors are widely distributed in nature. The side
chain plays an important role in binding of the flavin ring system to the protein
and therefore the majority of flavoproteins have a strong preference for either
FMN or FAD. On the other hand, riboflavin does not play a general role as a
cofactor in flavoenzymes. In addition to the noncovalent binding of the flavin
to the protein, covalent linkage to an amino acid residue via the 8- or 6-position
of the isoalloxazine ring system is also found (see Chapter 13). In all cases, the
mechanistically relevant moiety is the isoalloxazine ring system that serves as
a reversible reduction-oxidation catalyst in many biological redox processes
(for a review see: (1,2)). This is also the structural component of the flavin
cofactor that is responsible for light absorption in the UV and visible spectral
range giving rise to the yellow appearance of the flavin and of flavoproteins
(Latin: flavus = yellow). In the oxidized form of the flavin two peaks at ≈ 360
and ≈ 450 nm are observed (see Fig. 2). Method 1 describes a procedure to
determine the extinction coefficient for a flavin bound to a particular flavoprotein which is based on the known extinction coefficient for free FMN and
FAD (12,500 and 11,300 M–1 cm–1, respectively). Binding of the flavin to
the protein moiety alters the extinction coefficient covering a range from
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