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J. Biol. Chem., Vol. 282, Issue 27, 19773-19780, July 6, 2007

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S-Nitrosylation-induced Conformational Change in Blackfin Tuna Myoglobin^*

Eric R. Schreiter¹, María M. Rodríguez, Andrzej Weichsel, William R. Montfort, and Joseph Bonaventura^¶||

From the Protein Research Center, Department of Chemistry, University of Puerto Rico, Mayagüez, Puerto Rico 00681, Department of Biochemistry and Molecular Biophysics, University of Arizona, Tucson, Arizona 85721, ^¶Duke University Medical Center, Durham, North Carolina, 27710, and ^||Nicholas School of the Environment (SOE) Marine Laboratory, Beaufort, North Carolina, 28516

S-Nitrosylation is a post-translational protein modification that can alter the function of a variety of proteins. Despite the growing wealth of information that this modification may have important functional consequences, little is known about the structure of the moiety or its effect on protein tertiary structure. Here we report high-resolution x-ray crystal structures of S-nitrosylated and unmodified blackfin tuna myoglobin, which demonstrate that in vitro S-nitrosylation of this protein at the surface-exposed Cys-10 directly causes a reversible conformational change by "wedging" apart a helix and loop. Furthermore, we have demonstrated in solution and in a single crystal that reduction of the S-nitrosylated myoglobin with dithionite results in NO cleavage from the sulfur of Cys-10 and rebinding to the reduced heme iron, showing the reversibility of both the modification and the conformational changes. Finally, we report the 0.95-Å structure of ferrous nitrosyl myoglobin, which provides an accurate structural view of the NO coordination geometry in the context of a globin heme pocket.

Received for publication, February 15, 2007 , and in revised form, April 27, 2007.

The atomic coordinates and structure factors (code 2NRL, 2NRM, and 2NX0) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by Grants 5P20RR016439-05 (to J. B.) and HL62969 (to W. R. M.) from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Protein Research Center, Dept. of Chemistry, University of Puerto Rico, Mayagüez, PR, 00681. Tel.: 787-832-4040 (ext. 2348); Fax: 787-265-3849; E-mail: eric_sch{at}mit.edu.

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