NDLI: Heme-heme and heme-ligand interactions in the di-heme oxygen-reducing site of cytochrome bd from Escherichia coli revealed by nanosecond absorption spectroscopy

Content Provider	PubMed Central
Author	Rappaport, Fabrice Zhang, Jie Vos, Marten H. Gennis, Robert B. Borisov, Vitaliy B.
Copyright Year	2010
Abstract	Cytochrome bd is a terminal quinol:O2 oxidoreductase of respiratory chains of many bacteria. It contains three hemes, b 558, b 595, and d. The role of heme b 595 remains obscure. A CO photolysis/recombination study of the membranes of Escherichia coli containing either wild type cytochrome bd or inactive E445A mutant was performed using nanosecond absorption spectroscopy. We compared photoinduced changes of heme d-CO complex in one-electron-reduced, two-electron-reduced, and fully-reduced states of cytochromes bd. The line shape of spectra of photodissociation of one-electron-reduced and two-electron-reduced enzymes is strikingly different from that of the fully-reduced enzyme. The difference demonstrates that in the fully-reduced enzyme photolysis of CO from heme d perturbs ferrous heme b 595 causing loss of an absorption band centered at 435 nm, thus supporting interactions between heme b 595 and heme d in the di-heme oxygen-reducing site, in agreement with previous works. Photolyzed CO recombines with the fully-reduced enzyme monoexponentially with τ ~12 µs, whereas recombination of CO with one-electron-reduced cytochrome bd shows three kinetic phases, with τ ~14 ns, 14 µs, and 280 µs. The spectra of the absorption changes associated with these components are different in line shape. The 14 ns phase, absent in the fully-reduced enzyme, reflects geminate recombination of CO with part of heme d. The 14 µs component reflects bimolecular recombination of CO with heme d and electron backflow from heme d to hemes b in ~4% of the enzyme population. The final, 280 µs component, reflects return of the electron from hemes b to heme d and bimolecular recombination of CO in that population. The fact that even in the two-electron-reduced enzyme, a nanosecond geminate recombination is observed, suggests that namely the redox state of heme b 595, and not that of heme b 558, controls the pathway(s) by which CO migrates between heme d and the medium.
Related Links	http://dx.doi.org/10.1016/j.bbabio.2010.05.010
Ending Page	1664
Page Count	8
Starting Page	1657
File Format	PDF
ISSN	00052728
Journal	Biochimica et biophysica acta
Issue Number	9
Volume Number	1797
Language	English
Publisher Date	2010-09-01
Access Restriction	Open
Subject Keyword	Biophysics Cell Biology Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Biophysics

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