title: Interactions of Cu(B) with Carbon Monoxide in Cytochrome c Oxidase: Origin of the Anomalous Correlation between the Fe-CO and C-O Stretching Frequencies.
abstract: In heme-copper oxidases, the correlation curve between the iron-CO and C-O stretching vibrational modes (ν(Fe-CO) and ν(C-O), respectively) is anomalous as compared to the correlation in other heme proteins. To extend the correlation curve, the resonance Raman (RR) and infrared (IR) spectra of the CO adducts of cytochrome ba3 (ba3) from Thermus thermophilus were measured. The RR spectrum has two strong ν(Fe-CO) lines (508 and 515 cm(-1)) and a very weak line at 526 cm(-1), and the IR spectrum has three ν(C-O) lines (1966, 1973, and 1981 cm(-1)), indicating the presence of multiple conformers. Employing photodissociation methods, the ν(Fe-CO) RR and ν(C-O) IR lines were assigned to each conformer, enabling the establishment of a reliable inverse correlation curve for the ν(Fe-CO) versus the ν(C-O) stretching frequencies. To determine the molecular basis of the correlation, a series of DFT calculations on 6-coordinate porphyrin-CO compounds and a model of the binuclear center of the heme-copper oxidases were carried out. The calculations demonstrated that the copper unit model caused significant mixing among porphyrin-CO molecular orbitals (MOs) that contribute to the Fe-C and C-O bonding interactions, and also indicated the presence of mixing between the d(z)(2) orbital of the copper and MOs that are responsible for the ν(Fe-CO) vs ν(C-O) inverse correlation. Together, the spectroscopic and DFT results clarify the origin of the anomaly of ν(Fe-CO) and ν(C-O) frequencies in the heme-copper oxidases, a long-standing issue.
authors.affiliation: †Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
authors.forename: Tsuyoshi
authors.initials: T
authors.lastname: Egawa
authors.affiliation: †Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
authors.forename: Jonah
authors.initials: J
authors.lastname: Haber
authors.affiliation: ‡Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, United States.
authors.forename: James A
authors.initials: JA
authors.lastname: Fee
authors.affiliation: †Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
authors.forename: Syun-Ru
authors.initials: SR
authors.lastname: Yeh
authors.affiliation: †Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, United States.
authors.forename: Denis L
authors.initials: DL
authors.lastname: Rousseau
mesh_terms: D002244:Carbon / Q000737:chemistry; D002248:Carbon Monoxide / Q000737:chemistry; D003573:Cytochrome b Group / Q000737:chemistry; D003576:Electron Transport Complex IV / Q000737:chemistry*; D007501:Iron / Q000737:chemistry; D008956:Models, Chemical; D010100:Oxygen / Q000737:chemistry; D011166:Porphyrins / Q000737:chemistry; D013055:Spectrophotometry, Infrared; D013059:Spectrum Analysis, Raman; D016963:Thermus thermophilus
chemical_list: D003573:Cytochrome b Group; D011166:Porphyrins; D002244:Carbon; D002248:Carbon Monoxide; D007501:Iron; C058557:cytochrome ba3; D003576:Electron Transport Complex IV; D010100:Oxygen