The binding affinity of (S)-2-amino-6-nitrohexanoic acid to human arginase I was studied using surface plasmon resonance (K(d) = 60 microM), and the X-ray crystal structure of the enzyme-inhibitor complex was determined at 1.6 A resolution to reveal multiple nitro-metal coordination interactions.
(S)-2-amino-6-nitrohexanoic acid binds to human arginase i through multiple nitro-metal coordination interactions in the binuclear manganese cluster / Zakharian, T. Y.; DI COSTANZO, Luigi; Christianson, D. W.. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - 130:51(2008), pp. 17254-17255. [10.1021/ja807702q]
(S)-2-amino-6-nitrohexanoic acid binds to human arginase i through multiple nitro-metal coordination interactions in the binuclear manganese cluster
Di Costanzo Luigi;
2008
Abstract
The binding affinity of (S)-2-amino-6-nitrohexanoic acid to human arginase I was studied using surface plasmon resonance (K(d) = 60 microM), and the X-ray crystal structure of the enzyme-inhibitor complex was determined at 1.6 A resolution to reveal multiple nitro-metal coordination interactions.File in questo prodotto:
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