NDLI: Reconstruction of absolute absorption spectrum of reduced heme a in cytochrome c oxidase from bovine heart

Content Provider	Springer Nature Link
Author	Dyuba, A. V. Vygodina, T. V. Konstantiv, A. A.
Copyright Year	2013
Abstract	This paper presents a new experimental approach for determining the individual optical characteristics of reduced heme a in bovine heart cytochrome c oxidase starting from a small selective shift of the heme a absorption spectrum induced by calcium ions. The difference spectrum induced by Ca2+ corresponds actually to a first derivative (differential) of the heme a 2+ absolute absorption spectrum. Such an absolute spectrum was obtained for the mixed-valence cyanide complex of cytochrome oxidase (a 2+ a 3 3+ -CN) and was subsequently used as a basis spectrum for further procession and modeling. The individual absorption spectrum of the reduced heme a in the Soret region was reconstructed as the integral of the difference spectrum induced by addition of Ca2+. The spectrum of heme a 2+ in the Soret region obtained in this way is characterized by a peak with a maximum at 447 nm and half-width of 17 nm and can be decomposed into two Gaussians with maxima at 442 and 451 nm and half-widths of ∼10 nm (589 cm−1) corresponding to the perpendicularly oriented electronic π→π* transitions B 0x and B 0y in the porphyrin ring. The reconstructed spectrum in the Soret band differs significantly from the “classical” absorption spectrum of heme a 2+ originally described by Vanneste (Vanneste, W. H. (1966) Biochemistry, 65, 838–848). The differences indicate that the overall γ-band of heme a 2+ in cytochrome oxidase contains in addition to the B 0x and B 0y transitions extra components that are not sensitive to calcium ions, or, alternatively, that the Vanneste’s spectrum of heme a 2+ contains significant contribution from heme a 3 2+ . The reconstructed absorption band of heme a 2+ in the α-band with maximum at 605 nm and half-width of 18 nm (850 cm−1) corresponds most likely to the individual Q 0y transition of heme a, whereas the Q 0x transition contributes only weakly to the spectrum.
Starting Page	1358
Ending Page	1365
Page Count	8
File Format	PDF
ISSN	00062979
Journal	Biochemistry (Moscow)
Volume Number	78
Issue Number	12
e-ISSN	16083040
Language	English
Publisher	Pleiades Publishing
Publisher Date	2013-12-17
Publisher Place	Moscow
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	cytochrome c oxidase Ca2+ heme a absorption spectrum spectral shift Biochemistry Bioorganic Chemistry Microbiology Biomedicine general
Content Type	Text
Resource Type	Article
Subject	Biochemistry Biophysics Geriatrics and Gerontology

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