title: Crystal structures of oxidized and reduced forms of NADH peroxidase.
abstract: X-ray structural characterization of cysteine-sulfenic acid-containing proteins is one of the most defining approaches to characterizing this rapidly growing class of protein functional groups. Although outside the scope of this chapter, these structural analyses can lead to kinetic measurements in the crystal that allow intermediate states to be trapped, visualized, and studied. An understanding of the biochemistry of these reactive groups can be more fully gained by studying the localized protein environment in which these groups function. Increased perception of how elements of a protein can stabilize and contribute to modulation of function in these systems will allow novel means of enhancing or inhibiting function in important classes of protein molecules, including transcription factors and redox-regulated enzymes.
authors.affiliation: Department of Molecular Biology, Cell Biology, and Biochemistry, Department of Chemistry, Brown University, Providence, Rhode Island 02912, USA.
authors.forename: Joanne I
authors.initials: JI
authors.lastname: Yeh
authors.forename: Al
authors.initials: A
authors.lastname: Claiborne
mesh_terms: D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D055672:Static Electricity
chemical_list: D010544:Peroxidases; C021845:NAD+ peroxidase; D003545:Cysteine