title: Two conformations of the catalytic site in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides.
abstract: Resonance Raman spectra of the carbon monoxy derivative of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides show two distinct Fe-CO stretching modes (519 and 493 cm-1) at room temperature. The frequency of the mode at 519 cm-1 coincides with that of other terminal oxidases at neutral pH. Two C-O stretching modes, one at 1966 cm-1 and one at 1955 cm-1, are also found. The splitting of the C-O stretching mode is consistent with the FTIR spectra of cytochrome c oxidases at cryogenic temperatures in which two different conformations (alpha and beta) of the catalytic site of the enzyme are present. The splitting of both the Fe-CO and C-O stretching modes under our conditions indicates that these two forms of the enzyme are also present at room temperature, and with the additional information on the Fe-CO modes provided here, a structural origin for the two forms may be postulated. The alpha-form has the same general structure of the active site as mammalian oxidase, a structure in which the copper atom that is the part of the Fe-CuB binuclear site interacts strongly with the bound CO. We postulate that the copper atom exerts a strong polar or steric effect on the heme-bound CO, resulting in either compression of the Fe-CO bond or distortion of the Fe-CO moiety.(ABSTRACT TRUNCATED AT 250 WORDS)
authors.affiliation: AT&T Bell Laboratories, Murray Hill, New Jersey 07974, USA.
authors.forename: J
authors.initials: J
authors.lastname: Wang
authors.forename: S
authors.initials: S
authors.lastname: Takahashi
authors.forename: J P
authors.initials: JP
authors.lastname: Hosler
authors.forename: D M
authors.initials: DM
authors.lastname: Mitchell
authors.forename: S
authors.initials: S
authors.lastname: Ferguson-Miller
authors.forename: R B
authors.initials: RB
authors.lastname: Gennis
authors.forename: D L
authors.initials: DL
authors.lastname: Rousseau
mesh_terms: D001665:Binding Sites; D002248:Carbon Monoxide / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D003576:Electron Transport Complex IV / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D012242:Rhodobacter sphaeroides / Q000201:enzymology*; D017550:Spectroscopy, Fourier Transform Infrared; D013059:Spectrum Analysis, Raman
chemical_list: D002248:Carbon Monoxide; D007501:Iron; D003576:Electron Transport Complex IV