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By Alton Meister

Site visitors ATPases: A Superfamily of delivery Proteins working from Escherichia coli to people (G. Ames, et al.).

The breathing Burst Oxidase (B. Babior).

seasoned- and Antioxidant capabilities of Quinones and Quinone Reductase in Mammalian Cells (E. Cadenas & P. Hochstein).

The Redox facilities of Ribonucleotide Reductase of Escherichia coli (M. Fontecave, et al.).

lengthy diversity Intramolecular associated features within the Calcium shipping ATPase (G. Inesi, et al.).

Hydrogen-Bonding in Carbohydrates and Hydrate Inclusion Compounds (G. Jeffrey).

Methylation of mRNA (P. Narayan & F. Rottman).

Mammalian Nitric Oxide Synthases (D. Stuehr & O. Griffith).

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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 65

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1986b). The basis of multidrug resistance in mammalian cells: Homology with bacterial transport, Cell, 47, 323-324. Ames, G . -L. (1990a). Energetics of periplasmic transport systems: the histidine permease as a model system, Res. , 141, 341-348. Ames, G. -L. (1990b). Energetics of periplasmic transport systems. In “Bacterial Energetics” (T. A. Krulwich, ed). The Bacteria. Vol 12 (Acad. Press) pp 225246. Ames, G. -L. (1992). Bacterial periplasmic permeases as model systems for the superfamily of traffic ATPases which includes MDR and CFTR.

1991), these data show that its membrane association also interferes with the formation or accessibility of the ATP-binding site. In contrast to HisP’s behavior, HisQ does not exhibit a requirement for the presence of HisP for binding ATP. HisQ is labeled by 8-azido ATP in mutants lacking HisP entirely as well as it is in the wild type. Indeed, the ATP-binding activity of HisQ may possibly be necessary for the hypothetical “modification” of HisP. Strains producing mutant HisQ that cannot bind ATP would be useful to determine whether the lack of ATP-binding ability in HisQ has an effect on the ATP-binding site of HisP.

B i d . , 256, 560-562. Ames, G. -L. (1972). Components of histidine transport, in Biologicul Membranes. Proceedings of the 1972 ICN-UCLA Symposium in Molecular Biology, Fox, C. , Academic Press, New York, pp. 409-426. Ames, G. -L. (1985). The histidine transport system of Salmonella ryphimurium, in Current Topics in Membranes und Transport, Vol. 23, Academic Press, New York, pp. 103-119. Ames, G. -L. (l986a). Bacterial periplasmic transport systems: Structure, mechanism, and evolution, Ann. Rev.

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