Alpha and beta forms of cytochrome c oxidase observed in rat heart myocytes by low temperature Fourier transform infrared spectroscopy.

Fiamingo, Frank G.; Altschuld, Ruth A.; Alben, James O.

doi:10.1016/s0021-9258(18)69258-0

Cited by 36 publications

(22 citation statements)

References 38 publications

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“…The FTIR absorption lightminus-dark difference spectrum of the CO adduct of the aa 3type cytochrome c oxidase of R. sphaeroides is almost identical to that of the oxidase from bovine mitochondria (Shapleigh et al, 1992a). Oxidases from each of these organisms exhibit two molecular conformations, designated R and β (Fiamingo et al, 1986;Shapleigh et al, 1992a). In the aa 3 -type oxidase of R. sphaeroides, the FesCtO R form has a maximum at 1964 cm -1 , while the CusCtO R form is seen at 2060 cm -1 (Shapleigh et al, 1992a).…”

Section: Resultsmentioning

confidence: 95%

Polar Residues in Helix VIII of Subunit I of Cytochrome c Oxidase Influence the Activity and the Structure of the Active Site

et al. 1996

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The aa3-type cytochrome c oxidase from Rhodobacter sphaeroides is closely related to eukaryotic cytochrome c oxidases. Analysis of site-directed mutants identified the ligands of heme a, heme a3, and CuB [Hosler et al. (1993) J. Bioenerg. Biomembr. 25, 121-133], which have been confirmed by high-resolution structures of homologous oxidases [Iwata et al. (1995) Nature 376, 660; Tsukihara et al. (1995) Science 269, 1069; (1996) 272, 1136]. Since the protons used to form water originate from the inner side of the membrane, and the heme a3-CuB center is located near the outer surface, the protein must convey these substrate protons to the oxygen reduction site. Transmembrane helix VIII in subunit I is close to this site and contains several conserved polar residues that could function in a rate-determining proton relay system. To test this role, apolar residues were substituted for T352, T359, and K362 in helix VIII and the mutants were characterized in terms of activity and structure. Mutation of T352, near CuB, strongly decreases enzyme activity and disrupts the spectral properties of the heme a3-CuB center. Mutation of T359, below heme a3, substantially reduces oxidase activity with only minor effects on metal center structure. Two mutations of K362, approximately 15 A below the axial ligand of heme a3, are inactive, make heme a3 difficult to reduce, and cause changes in the resonance Raman signal specific for the iron-histidine bond to heme a3. The results are consistent with a key role for T352, T359, and K362 in oxidase activity and with the involvement of T359 and K362 in proton transfer through a relay system now plausibly identified in the crystal structure. However, the characteristics of the K362 mutants raise some questions about the assignment of this as the substrate proton channel.

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Section: Resultsmentioning

confidence: 95%

Polar Residues in Helix VIII of Subunit I of Cytochrome c Oxidase Influence the Activity and the Structure of the Active Site

et al. 1996

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“…5 A displays the redox FTIR spectra of cytochrome bo 3 recorded in the range of 1690-1990 cm 21 , using different light sources and reaction conditions. At ;1960 cm 21 , the adducts of CO with ferrous high-spin heme (Fiamingo et al, 1986;Hill et al, 1992;Shapleigh et al, 1992;Lemon et al, 1993;Einarsdottir et al, 1993;Rich and Breton, 2001) could be observed. CO release occurs under intense irradiation seen in the laser-induced spectrum (Fig.…”

Section: General Effect Of Photoirradiation On Ftir Spectra (Cytochrome Bo 3 )mentioning

confidence: 98%

Noninvasive Auto-Photoreduction Used as a Tool for Studying Structural Changes in Heme-Copper Oxidases by FTIR Spectroscopy

Bettinger¹,

Prutsch²,

Vogtt

et al. 2004

Biophysical Journal

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We demonstrate an efficient Fourier transform infrared (FTIR) spectroscopic method, termed "auto-photoreduction," that uses anaerobic photo-induced internal electron transfer to monitor reaction-initiated changes of heme-copper oxidases. It can be applied without the use of either expensive electrochemical equipment, or caged compounds, which cause significant background signals. At high irradiation power, carbon monoxide is released from high-spin heme a of cytochrome c oxidase and heme o from cytochrome bo(3). Photochemistry is initiated at wavelengths <355 nm, and the photochemical action spectrum has a maximum of 290 nm for cytochrome bo(3), which is consistent with the possible intermediate involvement of tyrosinate or an activated state of tyrosine. We propose that the final electron donors are proton channel water molecules. In the pH range of 4-9, the noninvasive auto-photoreduction method yields highly reproducible FTIR redox difference spectra within a broad range, resolving a number of vibrational changes outside the amide I region (1600-1640 cm(-1)). Furthermore, it provides details of redox-induced changes in the spectral region between 1600 and 1100 cm(-1). The auto-photoreduction method should be universally applicable to heme proteins.

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“…Interestingly, at cryogenic temperatures, after CO photodissociation only the transfer of CO from heme a 3 to Cu B is observed. 74, 75 Dyer et al took advantage of single-wavelength timeresolved infrared spectroscopy to present first evidence on CO binding to Cu B + at room temperature. 76 They observed the decay of Cu B + -CO species with a half-life of 1.5 ms and the subsequent rebinding of CO to the heme a 3 .…”

Section: Q Bmentioning

confidence: 99%

Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins

Radu

Schleeger

Bolwien

et al. 2009

Photochem Photobiol Sci

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The introduction of time-resolved Fourier transform infrared (FT-IR) spectroscopy to biochemistry opened the possibility of monitoring the catalytic mechanism of proteins along their reaction pathways. The infrared approach is very fruitful, particularly in the application to membrane proteins where NMR and X-ray crystallography are challenged by the size and protein hydrophobicity, as well as by their limited time-resolution. Here, we summarize the principles and experimental realizations of time-resolved FT-IR spectroscopy developed in our group and compare with aspects emerging from other laboratories. Examples of applications to retinal proteins and energy transduction complexes are reviewed, which emphasize the impact of time-resolved FT-IR spectroscopy on the understanding of protein reactions on the level of single bonds.

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Alpha and beta forms of cytochrome c oxidase observed in rat heart myocytes by low temperature Fourier transform infrared spectroscopy.

Cited by 36 publications

References 38 publications

Polar Residues in Helix VIII of Subunit I of Cytochrome c Oxidase Influence the Activity and the Structure of the Active Site

Polar Residues in Helix VIII of Subunit I of Cytochrome c Oxidase Influence the Activity and the Structure of the Active Site

Noninvasive Auto-Photoreduction Used as a Tool for Studying Structural Changes in Heme-Copper Oxidases by FTIR Spectroscopy

Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins

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