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Reorientation of cytochrome c₂ upon interaction with oppositely charged macromolecules probed by SR EPR: implications for the role of dipole moment to facilitate collisions in proper configuration for electron transfer

Control of the stereo-selectivity of styrene epoxidation by cytochrome P450 BM3 using structure-based mutagenesis

Circular dichroism spectra of cytochrome c oxidase

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Metallomics Vol - 3 Issue - 3

Metallomics Vol - 3 Issue - 2

Metallomics Vol -2

Metallomics Vol -1

Circular dichroism spectra of cytochrome c oxidase

Content Provider	Royal Society of Chemistry (RSC)
Author	Arutyunyan, Alexander M. Vygodina, Tatiana V. Kalinovich, Anastasia V. Dyuba, Artem V. Azarkina, Natalia V. Sharonov, Yuri A. Konstantinov, Alexander A.
Copyright Year	2011
Abstract	Circular dichroism spectra of bovine heart aa3-type cytochrome c oxidase have been studied with a major focus on the Soret band π → π* transitions, B0(x,y), in the two iron porphyrin groups of the enzyme. The spectra of the fully reduced and fully oxidized enzyme as well as of its carbon monoxide and cyanide complexes have been explored. In addition, CD spectra of the reduced and oxidized ba3-type cytochrome c oxidase from Thermus thermophilus were recorded for comparison. An attempt is made to interpret the CD spectra of cytochrome c oxidase with the aid of a classical model of dipole–dipole coupled oscillators taking advantage of the known 3D crystal structure of the enzyme. Simultaneous modeling of the CD and absorption spectra shows that in the bovine oxidase, the dipole–dipole interactions between the hemes a and a3, although contributing significantly, cannot account either for the lineshape or the magnitude of the experimental spectra. However, adding the interactions of the hemes with 22 aromatic amino acid residues located within 12 Å from either of the two heme groups can be used to model the CD curves for the fully reduced and fully oxidized oxidase with reasonable accuracy. Interaction of the hemes with the peptide bond transition dipoles is found to be insignificant. The modeling indicates that the CD spectra of cytochrome oxidase in both the reduced and oxidized states are influenced significantly by interaction with Tyr244 in the oxygen-reducing center of the enzyme. Hence, CD spectroscopy may provide a useful tool for monitoring the redox/ionization state of this residue. The modeling confirms wide energy splitting of the orthogonal Bx and By transitions in the porphyrin ring of heme a.
Starting Page	417
Ending Page	432
Page Count	16
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	3
Issue Number	4
Journal	Metallomics
DOI	10.1039/c0mt00099j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Cytochrome c oxidase Cyanide Spectroscopy Enzyme Peptide bond Oxidase Redox Orthogonality Circular dichroism Three-dimensional space Thermus thermophilus Porphyrin Classical mechanics Carboxylic acid Ionization Dipole Soret peak Carbon monoxide
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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Peculiarities of cyanide binding to the ba 3-type cytochrome oxidase from the thermophilic bacterium Thermus thermophilus

Investigation Of The O2 Reduction Mechanism And Ligand Access In Cytochrome C Oxidase From Thermus Thermophilus

Photobiochemical Production of Carbon Monoxide by Thermus thermophilus $ba_{3}-Cytochrome$ c Oxidase

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Time-resolved magnetic circular dichroism spectroscopy of photolyzed carbonmonoxy cytochrome c oxidase (cytochrome aa3).

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Proton Transfer in the K-Channel Analog of B-Type Cytochrome c Oxidase from Thermus thermophilus

Circular dichroism spectra of cytochrome c oxidase

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