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Article

Crystal structure of a NO-forming nitrite reductase mutant: an analog of a transition state in enzymatic reaction.

Biochemical and biophysical research communications - 14 Mar 2003

Liu Sheng-Quan, Chang Tschining, Liu Ming-Yih, LeGall Jean, Chang Wen-Chang, Zhang Ji-Ping, Liang Dong-Cai, Chang Wen-Rui

Abstract excerpt

I257E was obtained by site directed mutagenesis of nitrite reductase from Achromobacter cycloclastes. The mutant has no enzyme activity. Its crystal structure determined at 1.65A resolution shows that the side-chain carboxyl group of the mutated residue, Glu257, coordinates with the type 2 copper in the mutant and blocks the contact between the type 2 copper and its solvent channel, indicating that the...

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PMID: 12615072
DOI: 10.1016/s0006-291x(03)00166-9

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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