Conformation of the c552:aa3 electron transfer complex in Paracoccus denitrificans studied by EPR on oriented samples

Gérard Lipowski; Ursula Liebl; Bruno Guigliarelli; Wolfgang Nitschke; Barbara Schoepp-Cothenet

doi:10.1016/j.febslet.2006.09.038

Conformation of the c₅₅₂:aa₃ electron transfer complex in Paracoccus denitrificans studied by EPR on oriented samples

Gérard Lipowski
, Ursula Liebl
, Bruno Guigliarelli
, Wolfgang Nitschke
, Barbara Schoepp-Cothenet

Research output: Contribution to journal › Article › peer-review

Abstract

The EPR spectral parameters of aa₃ oxidase and cyt c₅₅₂ from Paracoccus denitrificans were studied in purified oxidase and enriched cyt c₅₅₂. The orientation of the g-tensors of hemes a and c₅₅₂ were determined on partially ordered membranes, enriched cyt c₅₅₂ and a c₅₅₂:aa₃ subcomplex. The known correlation of g-tensor to molecular axes in histidine/methionine ligated hemes permits us to position cyt c₅₅₂ with respect to the parent membrane. Taken together with previous data on the interaction surface between aa₃ oxidase and cyt c₅₅₂, these results allow us to arrive at a single conformation for the c₅₅₂:aa₃ electron transfer complex.

Original language	English
Pages (from-to)	5988-5992
Number of pages	5
Journal	FEBS Letters
Volume	580
Issue number	25
DOIs	https://doi.org/10.1016/j.febslet.2006.09.038
Publication status	Published - 30 Oct 2006

Keywords

Cytochrome c
Electron transfer
Paracoccus denitrificans
Supercomplex
aa oxidase

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10.1016/j.febslet.2006.09.038

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title = "Conformation of the c552:aa3 electron transfer complex in Paracoccus denitrificans studied by EPR on oriented samples",

abstract = "The EPR spectral parameters of aa3 oxidase and cyt c552 from Paracoccus denitrificans were studied in purified oxidase and enriched cyt c552. The orientation of the g-tensors of hemes a and c552 were determined on partially ordered membranes, enriched cyt c552 and a c552:aa3 subcomplex. The known correlation of g-tensor to molecular axes in histidine/methionine ligated hemes permits us to position cyt c552 with respect to the parent membrane. Taken together with previous data on the interaction surface between aa3 oxidase and cyt c552, these results allow us to arrive at a single conformation for the c552:aa3 electron transfer complex.",

keywords = "Cytochrome c, Electron transfer, Paracoccus denitrificans, Supercomplex, aa oxidase",

author = "G{\'e}rard Lipowski and Ursula Liebl and Bruno Guigliarelli and Wolfgang Nitschke and Barbara Schoepp-Cothenet",

year = "2006",

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doi = "10.1016/j.febslet.2006.09.038",

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T1 - Conformation of the c552:aa3 electron transfer complex in Paracoccus denitrificans studied by EPR on oriented samples

AU - Lipowski, Gérard

AU - Liebl, Ursula

AU - Guigliarelli, Bruno

AU - Nitschke, Wolfgang

AU - Schoepp-Cothenet, Barbara

PY - 2006/10/30

Y1 - 2006/10/30

N2 - The EPR spectral parameters of aa3 oxidase and cyt c552 from Paracoccus denitrificans were studied in purified oxidase and enriched cyt c552. The orientation of the g-tensors of hemes a and c552 were determined on partially ordered membranes, enriched cyt c552 and a c552:aa3 subcomplex. The known correlation of g-tensor to molecular axes in histidine/methionine ligated hemes permits us to position cyt c552 with respect to the parent membrane. Taken together with previous data on the interaction surface between aa3 oxidase and cyt c552, these results allow us to arrive at a single conformation for the c552:aa3 electron transfer complex.

AB - The EPR spectral parameters of aa3 oxidase and cyt c552 from Paracoccus denitrificans were studied in purified oxidase and enriched cyt c552. The orientation of the g-tensors of hemes a and c552 were determined on partially ordered membranes, enriched cyt c552 and a c552:aa3 subcomplex. The known correlation of g-tensor to molecular axes in histidine/methionine ligated hemes permits us to position cyt c552 with respect to the parent membrane. Taken together with previous data on the interaction surface between aa3 oxidase and cyt c552, these results allow us to arrive at a single conformation for the c552:aa3 electron transfer complex.

KW - Cytochrome c

KW - Electron transfer

KW - Paracoccus denitrificans

KW - Supercomplex

KW - aa oxidase

UR - https://www.scopus.com/pages/publications/33750058262

U2 - 10.1016/j.febslet.2006.09.038

DO - 10.1016/j.febslet.2006.09.038

M3 - Article

C2 - 17052714

AN - SCOPUS:33750058262

SN - 0014-5793

VL - 580

SP - 5988

EP - 5992

JO - FEBS Letters

JF - FEBS Letters

IS - 25

ER -

Conformation of the c₅₅₂:aa₃ electron transfer complex in Paracoccus denitrificans studied by EPR on oriented samples

Abstract

Keywords

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