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Molybdenum enzymes crystallographic studies

From recent x-ray crystallographic studies of both molybdenum and tungsten enzymes, MPT is now known to be a C(6)-substituted 5,6-dihydropterin that is covalently alkoxylated at the C(7) position by the alcohol of the 1,2-enedithio-late side chain (Eq. 1) [39],... [Pg.84]

Thanks to several protein crystallographic studies and a wealth of spectroscopic information, we now have a good basis for understanding the structure-function relationships of the molybdenum and tungsten enzymes. In each... [Pg.541]

There are several recent reviews of the molybdenum and tungsten enzymes [4-6,23,26-36], In this chapter, we first define the metallocofactors and offer a compilation of the enzymes and their diverse activities. We then focus on the active-site structures, highlighting the confluence of crystallographic and spectroscopic studies. This is followed by a discussion of pertainent spectroscopic, structural, reactivity, and theoretical model studies. We then turn our attention to the mechanisms of catalytic activity of the molybdenum and tungsten enzymes. [Pg.83]


See other pages where Molybdenum enzymes crystallographic studies is mentioned: [Pg.106]    [Pg.117]    [Pg.132]    [Pg.110]    [Pg.460]    [Pg.464]    [Pg.114]    [Pg.959]    [Pg.1426]    [Pg.3265]    [Pg.467]    [Pg.354]    [Pg.94]    [Pg.165]    [Pg.169]    [Pg.174]   
See also in sourсe #XX -- [ Pg.106 ]




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Crystallographic studies

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