Less Common Metals in Proteins and Nucleic Acid Probes by Michael J. Maroney, Gerard Davidson (auth.)

By Michael J. Maroney, Gerard Davidson (auth.)

Some of the extra attention-grabbing components within the chemistry of existence are much less typically occuring ones comparable to nickel and molybdenum. This quantity elucidates the chemistry of those parts in very important enzymes and in addition explores the chemistry of parts that don't in general happen in organic molecules, yet are invaluable in probing their constitution and serve as. issues comprise: Acquisition and delivery of Ni. Mechanistic motion of Ni in a large choice of enzymes. Multielectron redox platforms related to pterins in proteins. Chemistry of the pterin and flavin complexes of Mo, Fe, Cu and Ru ions. substitute of iron in transferrin by way of a few different steel ions. Use of polypyridyl complexes of ruthenium and different transition metals as probes of nucleic acid constitution via photochemical reactions.

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14 is consistent with the fact that the conversion of Credl and Cred2 occurs upon exposure to CO, is kinetically viable, occurs at a potential that is near the CO/COz reduction potential (-520 mV), and is associated with an inherently two-electron redox process (see above). However, the nature of the Credl/Cred2 interconversion is not clear and might be associated with the reduction of an unknown redox site, or a conformational change rather than a reduction of Credl [154]. That CO2 is bound to Cluster-C is supported by the ability of CO2 to affect the epr spectrum of Cred~ and to facilitate the Credl/Cred2 conversion [154].

Zerner et al. originally proposed that Cys319 was the acid group. However, Cys319 is not required for catalysis. Studies involving site-directed mutagenesis of Cys319 reveal that this residue can be changed and the enzyme still has activity [84]. In particular, the C319A mutant retains 48% of the wild-type activity and exhibits only a slight increase in Kin. Structural studies of C319 mutants show that the effects of replacing Cys319 are minor and involve primarily changes in the structure of the water molecules in the active site, and the mobility and position of the active site flap containing Cys319 [70].

Rubrum, C. thermoaceticum, and other enzymes, strongly points to a common structure for the site of CO oxidation [143]. Taken together, all of the available data support a structure such as shown in Fig. 13. The presence of S-donor ligands in the coordination environment of Ni The Structure and Function of Nickel Sites 35 Cys I S S ~ F e I O/NCys O/NIt' NiI ~,~ -- ~ f u. Cys Cluster C cy , Cys I S S Fe O/N/t," . , , \ S ~ =[~ JI _4 ~N,O ~1 ~ I . Cy s / Cluster A Fig. 13. Top: Model for the structure of Cluster-C in CODH.

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