Abate

Arakawa

Aslund

Bauer

Claiborne

E. I. Solomon

F. Sun

Giles

Gray

Hadt

J. S. Woertink

J.-L. Zhang

Kovacs

Lancaster

M. J. Nilges

Michalek

Murakami

N. A. Sieracki

R. G. Hadt

Rehder

S. Tian

Tsai

Y. Lu

Significance
          
            Posttranslational modification of cysteinyl thiolate to sulfenate has been found to play important roles in biology, such as redox signaling, and enzyme and gene regulation. Nitrile hydratase and thiocyanate hydrolase with cobalt and iron cofactors are the few known metalloenzymes requiring sulfenate coordination for reactivity. No other metal ions have been found to stably bind sulfenate in a biological context. Here we report a copper–sulfenate complex characterized in a protein environment, formed at the active site of a cavity mutant of
            Pseudomonas aeruginosa
            azurin. Computational studies strongly suggest that noncovalent interactions in the secondary coordination sphere are critical in stabilizing this species.
          </jats:p

Nathan A. Sieracki

Shiliang Tian

Ryan G. Hadt

Jun-Long Zhang

Julia S. Woertink

Mark J. Nilges

Furong Sun

Edward I. Solomon

Yi Lu

Crossref

Proceedings of the National Academy of Sciences

Copper–sulfenate complex from oxidation of a cavity mutant of
            <i>Pseudomonas aeruginosa</i>
            azurin

Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin

Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin

Abstract

Similar works

Full text

Available Versions

Crossref