Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: The Fe-to-Fe distance between hemes d and b595 is 10 Å

Alexander M. Arutyunyan, Vitaliy B. Borisov, Vladimir I. Novoderezhkin, Josh Ghaim, Jie Zhang, Robert B. Gennis, Alexander A. Konstantinov

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Absorption and circular dichroism (CD) spectra of cytochrome bd from Escherichia coli have been compared for the wild type enzyme and an inactive mutant in which a highly conserved E445 in subunit I has been replaced by alanine [Zhang, J., Hellwig, P., Osborne, J. P., Huang, H. W., Moenne-Loccoz, P., Konstantinov, A. A., and Gennis, R. B. (2001) Biochemistry 40, 8548-8556]. The absorption bands of ferrous heme b595 are absent from the spectrum of the dithionite-reduced E445A form of cytochrome bd. The difference between the spectra of the dithionite-reduced WT and E445A enzymes indicates that in the mutant, heme b595 is present but is not reducible by dithionite. Cytochrome bd reveals intense CD signals dominated by heme d, with almost no contribution from heme b595 or heme b558. The CD spectrum of the reduced wild type enzyme in the Soret band indicates strong excitonic interactions between ferrous heme d and ferrous heme b595, and these interactions are not observed in dithionite-reduced E445A mutant, in which heme b595 remains in the ferric state. Modeling the excitonic interactions in both absorption and CD spectra has been carried out, yielding an estimate of the Fe-to-Fe distance between heme d and heme b595 of about 10 Å. The physical proximity supports the hypothesis that heme d and heme b595 can form a di-heme oxygen reducing site, a unique structure for respiratory oxidases.

Original languageEnglish (US)
Pages (from-to)1752-1759
Number of pages8
JournalBiochemistry
Volume47
Issue number6
DOIs
StatePublished - Feb 12 2008
Externally publishedYes

Fingerprint

Oxidoreductases
Dithionite
Oxygen
Circular Dichroism
Cytochromes
Heme
Enzymes
Biochemistry
heme d
heme b(595)
Alanine
Escherichia coli
Absorption spectra

ASJC Scopus subject areas

  • Biochemistry

Cite this

Arutyunyan, A. M., Borisov, V. B., Novoderezhkin, V. I., Ghaim, J., Zhang, J., Gennis, R. B., & Konstantinov, A. A. (2008). Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: The Fe-to-Fe distance between hemes d and b595 is 10 Å. Biochemistry, 47(6), 1752-1759. https://doi.org/10.1021/bi701884g

Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase : The Fe-to-Fe distance between hemes d and b595 is 10 Å. / Arutyunyan, Alexander M.; Borisov, Vitaliy B.; Novoderezhkin, Vladimir I.; Ghaim, Josh; Zhang, Jie; Gennis, Robert B.; Konstantinov, Alexander A.

In: Biochemistry, Vol. 47, No. 6, 12.02.2008, p. 1752-1759.

Research output: Contribution to journalArticle

Arutyunyan, AM, Borisov, VB, Novoderezhkin, VI, Ghaim, J, Zhang, J, Gennis, RB & Konstantinov, AA 2008, 'Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: The Fe-to-Fe distance between hemes d and b595 is 10 Å', Biochemistry, vol. 47, no. 6, pp. 1752-1759. https://doi.org/10.1021/bi701884g
Arutyunyan, Alexander M. ; Borisov, Vitaliy B. ; Novoderezhkin, Vladimir I. ; Ghaim, Josh ; Zhang, Jie ; Gennis, Robert B. ; Konstantinov, Alexander A. / Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase : The Fe-to-Fe distance between hemes d and b595 is 10 Å. In: Biochemistry. 2008 ; Vol. 47, No. 6. pp. 1752-1759.
@article{c92940b26235417d88f9721655be0dde,
title = "Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase: The Fe-to-Fe distance between hemes d and b595 is 10 {\AA}",
abstract = "Absorption and circular dichroism (CD) spectra of cytochrome bd from Escherichia coli have been compared for the wild type enzyme and an inactive mutant in which a highly conserved E445 in subunit I has been replaced by alanine [Zhang, J., Hellwig, P., Osborne, J. P., Huang, H. W., Moenne-Loccoz, P., Konstantinov, A. A., and Gennis, R. B. (2001) Biochemistry 40, 8548-8556]. The absorption bands of ferrous heme b595 are absent from the spectrum of the dithionite-reduced E445A form of cytochrome bd. The difference between the spectra of the dithionite-reduced WT and E445A enzymes indicates that in the mutant, heme b595 is present but is not reducible by dithionite. Cytochrome bd reveals intense CD signals dominated by heme d, with almost no contribution from heme b595 or heme b558. The CD spectrum of the reduced wild type enzyme in the Soret band indicates strong excitonic interactions between ferrous heme d and ferrous heme b595, and these interactions are not observed in dithionite-reduced E445A mutant, in which heme b595 remains in the ferric state. Modeling the excitonic interactions in both absorption and CD spectra has been carried out, yielding an estimate of the Fe-to-Fe distance between heme d and heme b595 of about 10 {\AA}. The physical proximity supports the hypothesis that heme d and heme b595 can form a di-heme oxygen reducing site, a unique structure for respiratory oxidases.",
author = "Arutyunyan, {Alexander M.} and Borisov, {Vitaliy B.} and Novoderezhkin, {Vladimir I.} and Josh Ghaim and Jie Zhang and Gennis, {Robert B.} and Konstantinov, {Alexander A.}",
year = "2008",
month = "2",
day = "12",
doi = "10.1021/bi701884g",
language = "English (US)",
volume = "47",
pages = "1752--1759",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "6",

}

TY - JOUR

T1 - Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase

T2 - The Fe-to-Fe distance between hemes d and b595 is 10 Å

AU - Arutyunyan, Alexander M.

AU - Borisov, Vitaliy B.

AU - Novoderezhkin, Vladimir I.

AU - Ghaim, Josh

AU - Zhang, Jie

AU - Gennis, Robert B.

AU - Konstantinov, Alexander A.

PY - 2008/2/12

Y1 - 2008/2/12

N2 - Absorption and circular dichroism (CD) spectra of cytochrome bd from Escherichia coli have been compared for the wild type enzyme and an inactive mutant in which a highly conserved E445 in subunit I has been replaced by alanine [Zhang, J., Hellwig, P., Osborne, J. P., Huang, H. W., Moenne-Loccoz, P., Konstantinov, A. A., and Gennis, R. B. (2001) Biochemistry 40, 8548-8556]. The absorption bands of ferrous heme b595 are absent from the spectrum of the dithionite-reduced E445A form of cytochrome bd. The difference between the spectra of the dithionite-reduced WT and E445A enzymes indicates that in the mutant, heme b595 is present but is not reducible by dithionite. Cytochrome bd reveals intense CD signals dominated by heme d, with almost no contribution from heme b595 or heme b558. The CD spectrum of the reduced wild type enzyme in the Soret band indicates strong excitonic interactions between ferrous heme d and ferrous heme b595, and these interactions are not observed in dithionite-reduced E445A mutant, in which heme b595 remains in the ferric state. Modeling the excitonic interactions in both absorption and CD spectra has been carried out, yielding an estimate of the Fe-to-Fe distance between heme d and heme b595 of about 10 Å. The physical proximity supports the hypothesis that heme d and heme b595 can form a di-heme oxygen reducing site, a unique structure for respiratory oxidases.

AB - Absorption and circular dichroism (CD) spectra of cytochrome bd from Escherichia coli have been compared for the wild type enzyme and an inactive mutant in which a highly conserved E445 in subunit I has been replaced by alanine [Zhang, J., Hellwig, P., Osborne, J. P., Huang, H. W., Moenne-Loccoz, P., Konstantinov, A. A., and Gennis, R. B. (2001) Biochemistry 40, 8548-8556]. The absorption bands of ferrous heme b595 are absent from the spectrum of the dithionite-reduced E445A form of cytochrome bd. The difference between the spectra of the dithionite-reduced WT and E445A enzymes indicates that in the mutant, heme b595 is present but is not reducible by dithionite. Cytochrome bd reveals intense CD signals dominated by heme d, with almost no contribution from heme b595 or heme b558. The CD spectrum of the reduced wild type enzyme in the Soret band indicates strong excitonic interactions between ferrous heme d and ferrous heme b595, and these interactions are not observed in dithionite-reduced E445A mutant, in which heme b595 remains in the ferric state. Modeling the excitonic interactions in both absorption and CD spectra has been carried out, yielding an estimate of the Fe-to-Fe distance between heme d and heme b595 of about 10 Å. The physical proximity supports the hypothesis that heme d and heme b595 can form a di-heme oxygen reducing site, a unique structure for respiratory oxidases.

UR - http://www.scopus.com/inward/record.url?scp=38949194251&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=38949194251&partnerID=8YFLogxK

U2 - 10.1021/bi701884g

DO - 10.1021/bi701884g

M3 - Article

C2 - 18205406

AN - SCOPUS:38949194251

VL - 47

SP - 1752

EP - 1759

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 6

ER -