ArticleBiophysical journal2002
Transient binding of CO to Cu(B) in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: a time-resolved step-scan Fourier transform infrared investigation.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 87 citations in OpenAlex.
- Role of Protonation States in the Stability of Molecular Dynamics Simulations of High-Resolution Membrane Protein Structures.The journal of physical chemistry. B · 2024Article
- Membrane Protein Activity Induces Specific Molecular Changes in Nanodiscs Monitored by FTIR Difference Spectroscopy.Frontiers in molecular biosciences · 2022Article
- Quantification of Local Electric Field Changes at the Active Site of CytochromeFrontiers in chemistry · 2021Article
- Probing the Proton-Loading Site of CytochromeMolecules (Basel, Switzerland) · 2020Article
- Comparison Between O and OH Intermediates of CytochromeFrontiers in chemistry · 2020Article
- Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy.Biochimica et biophysica acta. Bioenergetics · 2018Article
- ns-μs Time-Resolved Step-Scan FTIR of ba₃ Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927.International journal of molecular sciences · 2016Article
- Structural Changes and Proton Transfer in Cytochrome c Oxidase.Scientific reports · 2015Article
- Mutation of a single residue in the ba3 oxidase specifically impairs protonation of the pump site.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Phase-sensitive detection in modulation excitation spectroscopy applied to potential induced electron transfer in cytochrome c oxidase.Applied spectroscopy · 2014Article
- Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides.Biophysical journal · 2013Article
- An engineered heme-copper center in myoglobin: CO migration and binding.Biochimica et biophysica acta · 2013Article
- Far infrared radiation (FIR): its biological effects and medical applications.Photonics & lasers in medicine · 2012Article
- Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli.Biochimica et biophysica acta · 2011Article
- Time-resolved flow-flash FT-IR difference spectroscopy: the kinetics of CO photodissociation from myoglobin revisited.Analytical and bioanalytical chemistry · 2009Article
- Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Probing the Q-proton pathway of ba3-cytochrome c oxidase by time-resolved Fourier transform infrared spectroscopy.Biophysical journal · 2004Article
- Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The redox-driven proton pump cytochrome c oxidase is that enzymatic machinery of the respiratory chain that transfers electrons from cytochrome c to molecular oxygen and thereby splits molecular oxygen to form water. To investigate the reaction mechanism of cytochrome c oxidase on the single vibrational level, we used time-resolved step-scan Fourier transform infrared spectroscopy and studied the dynamics of the reduced enzyme after photodissociation of bound carbon monoxide across the mid-infrared range (2300-950 cm(-1)). Difference spectra of the bovine complex were obtained at -20 degrees C with 5 micros time resolution. The data demonstrate a dynamic link between the transient binding of CO to Cu(B) and changes in hydrogen bonding at the functionally important residue E(I-286). Variation of the pH revealed that the pK(a) of E(I-286) is >9.3 in the fully reduced CO-bound oxidase. Difference spectra of cytochrome c oxidase from beef heart are compared with those of the oxidase isolated from Rhodobacter sphaeroides. The bacterial enzyme does not show the environmental change in the vicinity of E(I-286) upon CO dissociation. The characteristic band shape appears, however, in redox-induced difference spectra of the bacterial enzyme but is absent in redox-induced difference spectra of mammalian enzyme. In conclusion, it is demonstrated that the dynamics of a large protein complex such as cytochrome c oxidase can be resolved on the single vibrational level with microsecond Fourier transform infrared spectroscopy. The applied methodology provides the basis for future investigations of the physiological reaction steps of this important enzyme.
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