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On the Coordination and Oxidation States of the Active-Site Copper Ion in Prokaryotic Cu,Zn Superoxide Dismutases

โœ Scribed by M.E. Stroppolo; S. Nuzzo; A. Pesce; C. Rosano; A. Battistoni; M. Bolognesi; S. Mobilio; A. Desideri


Book ID
115582583
Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
89 KB
Volume
249
Category
Article
ISSN
0006-291X

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The analogous reaction of diSchiff base
โœ Dirk Deters; Ulrich Weser ๐Ÿ“‚ Article ๐Ÿ“… 1995 ๐Ÿ› Springer Netherlands ๐ŸŒ English โš– 377 KB

In addition to the well known catalytically accelerated O2 dismutation, Cu2Zn2 superoxide dismutase (SOD) reversibly reduces NO to NO-with the consequence of a prolonged half-life of NO. This alternative reactivity was examined in the presence of the intact CuZn enzyme and a diSchiff base copper com