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Cofactor F-430

The chemical and spectroscopic properties of the cofactor F-430 have been reviewed [98,99], The structure of the macrocycle (Figure 4) was elucidated by x-ray crystallography and NMR spectroscopy [100], The free cofactor, which is present in substantial amounts in the cells, has an absorption maximum at 430 nm, hence its name. In the enzyme, the absorption maximum is blue shifted to 420 nm. The pentamethyl ester of F-430 is soluble in organic solvents and can be reduced to the Ni(I) state under aprotic conditions, resulting in an absorption peak shift to 382 nm [101], or can be oxidized to the Ni(III) state, giving an absorption peak at 368 nm [102],... [Pg.248]

With the possible exception of the redox enzymes cytochrome P-450 (iron) and the methanogenic bacterial cofactor F-430 (nickel) [5-7], the cobalamines are the only... [Pg.328]

Step by step introduction of more effective ways of handling cytoplasmic chemistry, using coenzymes and special metal cofactors, e.g. haem (Fe), vitamin B12(Co), F-430(Ni), chlorophyll(Mg) and Moco(Mo). [Pg.268]

Corphin is the F-430 cofactor found in methyl-coenzyme M reductase, a nickel-containing enzyme that participates in the conversion of carbon dioxide to methane in methanogenic bacteria. The nickel ion in F-430 is coordinated by the tetrahydrocorphin ligand, which contains structural elements of both porphyrins and corrins. [Pg.170]

NF-F 430 reacting directly with MeS-CoM before/after the substrate activation, the role of the thiol cofactor HS-HTP, and the reason(s) for the enzyme specifically directing the C-S bond cleavage to the Me-S bond of Me-CoM are the principal questions to be resolved to understand how the enzyme methyl coenzyme M reductase functions. [Pg.2902]

The nickel-containing factor F 430 (134) provides an example of how nature exploits the reactivity of organometallic compounds, as is the case with vitamin B12. Factor F 430 (134) plays a key role as cofactor for the coenzyme M reductase of primitive methanogenic bacteria in the formation of methane from 2-(methylthio)-ethanesulfonate (86). The structural elucidation of factor F 430 (134) is based on a combination of classical spectroscopic methods, chemical degradation, and biosynthetic studies with C-labelled precursors 83a,b). These biosynthetic investigations will be addressed in section 8.2. Chemical degradation products obtained by ozonolysis of factor F 430 (134) allowed the determination of the absolute configuration by comparison with reference compounds derived from chlorophyll a (2) and vitamin B12 (4) 83a,b). [Pg.33]

The largest body of work is devoted to nickel (II) F-430, the hydrocorphin cofactor of methyl coenzyme M reductase from methanogenic bacteria... [Pg.32]


See other pages where Cofactor F-430 is mentioned: [Pg.248]    [Pg.250]    [Pg.248]    [Pg.250]    [Pg.250]    [Pg.251]    [Pg.61]    [Pg.7]   


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