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Crystal structures of oxidized and reduced forms of NADH peroxidase.
Yeh, Joanne I; Claiborne, Al.
  • Yeh JI; Department of Molecular Biology, Cell Biology, and Biochemistry, Department of Chemistry, Brown University, Providence, Rhode Island 02912, USA.
Methods Enzymol ; 353: 44-54, 2002.
Article en En | MEDLINE | ID: mdl-12078517
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.
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Banco de datos: MEDLINE Asunto principal: Peroxidasas Tipo de estudio: Prognostic_studies Idioma: En Año: 2002 Tipo del documento: Article
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Banco de datos: MEDLINE Asunto principal: Peroxidasas Tipo de estudio: Prognostic_studies Idioma: En Año: 2002 Tipo del documento: Article