Structure Of Cytochrome Oxidase Redox Centers in Native and Modified Forms: An EXAFS Study

B. Chance, Linda S Powers

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

This chapter discusses the homologies of cytochrome oxidase and oxygen that transport pigments of the electron transport components, such as cytochrome c peroxidase and catalases, and the other oxidases. The extended X-ray absorption fine structure (EXAFS) technique obtained with a synchrotron light source affords a method for measuring scalar distances of the nearest neighbor ligands of metal atoms in oxygen transport pigments and redox catalysts and is particularly effective in those involving binuclear metal centers. Rapid progress has been made in the application of EXAFS to structural problems of important oxygen transport pigments and metal enzymes. At present, X-ray absoption spectroscopy is being used to determine the distances between Fe and Cu atoms of the redox center of cytochrome oxidase under conditions that ensure sample integrity even under rigorous irradiation conditions and most recently to identify the pulsed or oxygenated oxidase as having a reaction center that retains a 3.84 ± 0.05 Å Fe-Cu distance but it lacks a bridging S atom found in the resting oxidized form.

Original languageEnglish (US)
Pages (from-to)1-19
Number of pages19
JournalCurrent Topics in Bioenergetics
Volume14
Issue numberC
DOIs
StatePublished - Jan 1 1985
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics

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