<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Pinakoulaki E</dc:creator>
  <dc:creator>Soulimane T</dc:creator>
  <dc:creator>Varotsis C</dc:creator>
  <dc:date>2002</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Fourier transform infrared (FTIR) and step-scan time-resolved FTIR difference spectra are reported for the [carbonmonoxy]cytochrome caa(3) from Thermus thermophilus. A major C-O mode of heme a(3) at 1958 cm(-1) and two minor modes at 1967 and 1975 cm(-1) (7:1:1) have been identified at room temperature and remained unchanged in H(2)O/D(2)O exchange. The observed C-O frequencies are 10 cm(-1) higher than those obtained previously at 21 K (Einarsdóttir, O., Killough, P. M., Fee, J. A., and Woodruff, W. H. (1989) J. Biol. Chem. 264, 2405-2408). The time-resolved FTIR data indicate that the transient Cu(B)(1+)-CO complex is formed at room temperature as revealed by the CO stretching mode at 2062 cm(-1). Therefore, the caa(3) enzyme is the only documented member of the heme-copper superfamily whose binuclear center consists of an a(3)-type heme of a beta-form and a Cu(B) atom of an alpha-form. These results illustrate that the properties of the binuclear center in other oxidases resulting in the alpha-form are not required for enzymatic activity. Dissociation of the transient Cu(B)(1+)-CO complex is biphasic. The rate of decay is 2.3 x 10(4) s(-1) (fast phase, 35%) and 36.3 s(-1) (slow phase, 65%). The observed rate of rebinding to heme a(3) is 34.1 s(-1). The implications of these results with respect to the molecular motions that are general to the photodynamics of the binuclear center in heme-copper oxidases are discussed.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.ch/global/documents/278382</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.1074/jbc.M205568200</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/12107185</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>The Journal of biological chemistry. - 2002</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Binding Sites</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Biochemical Phenomena</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Biochemistry</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Cytochrome c Group</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Cytochromes a</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Cytochromes a3</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">Electron Transport Complex IV</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Escherichia coli</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Heme</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Light</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Protein Binding</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Protein Conformation</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Spectroscopy, Fourier Transform Infrared</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Temperature</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Thermus thermophilus</dc:subject>
  <dc:title xmlns:ns16="xml" ns16:lang="en">Fourier transform infrared (FTIR) and step-scan time-resolved FTIR spectroscopies reveal a unique active site in cytochrome caa3 oxidase from Thermus thermophilus.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>