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Molybdo proteins

By an inspection of Table 3 some qualitative predictions can be made. Strong coupling is expected in copper-proteins, particularly in pseudo-tetrahedral sites (the so-called blue centers), in low-spin iron(III) and high-spin iron(II) proteins and molybdo-proteins, where the high strong formal charge provides large e values ). [Pg.81]

As seen from its amino acid sequence, the catalytic subunit PsrA of polysulfide reductase belongs to the DMSO reductase family of molybdo-oxidoreductases [26,29]. The structure of several single-subunit enzymes of this family is known. As a rule, the molybdenum ion coordinated by two MGD molecules appears to be the electron donor or acceptor to the respective substrate in these enzymes. A cavity extending from the surface of the protein to the molybdenum close to its center is seen in all structures. The substrates probably reach the active site near the molybdenum through this cavity, and the products are released at the surface through the cavity. With the assumption that PsrA... [Pg.115]


See other pages where Molybdo proteins is mentioned: [Pg.389]    [Pg.371]    [Pg.278]    [Pg.389]    [Pg.371]    [Pg.278]    [Pg.151]    [Pg.253]    [Pg.389]    [Pg.893]    [Pg.44]    [Pg.378]    [Pg.157]    [Pg.893]    [Pg.389]    [Pg.82]    [Pg.3930]    [Pg.374]   
See also in sourсe #XX -- [ Pg.278 ]




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