Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286

Ahmet S. Vakkasoglu; Joel E. Morgan; Dan Han; Ashtamurthy S. Pawate; Robert B. Gennis

doi:10.1016/j.febslet.2006.07.036

Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286

Ahmet S. Vakkasoglu, Joel E. Morgan, Dan Han, Ashtamurthy S. Pawate, Robert B. Gennis

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

Abstract

Mutants that decouple the proton pump of cytochrome c oxidase from Rhodobacter sphaeroides are postulated to do so by increasing the pK_a of glutamate 286, which is 20 Å away. The possibility that a conformational change near E286 is induced by the decoupling mutations (N139D and N207D) was investigated by FTIR difference spectroscopy. In both decoupled mutants, the reduced-minus-oxidized FTIR difference spectra show a shift of 2 cm^-1 to lower frequency of the band resulting from the absorbance of E286 in the oxidized enzyme. The decoupling mutants may influence E286 by altering the chain of water molecules which runs from the site of the mutations to E286.

Original language	English (US)
Pages (from-to)	4613-4617
Number of pages	5
Journal	FEBS Letters
Volume	580
Issue number	19
DOIs	https://doi.org/10.1016/j.febslet.2006.07.036
State	Published - Aug 21 2006

Keywords

Conformation
FTIR
Glutamate
Oxidase
Proton pump
Water

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Online availability

10.1016/j.febslet.2006.07.036

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title = "Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286",

abstract = "Mutants that decouple the proton pump of cytochrome c oxidase from Rhodobacter sphaeroides are postulated to do so by increasing the pKa of glutamate 286, which is 20 {\AA} away. The possibility that a conformational change near E286 is induced by the decoupling mutations (N139D and N207D) was investigated by FTIR difference spectroscopy. In both decoupled mutants, the reduced-minus-oxidized FTIR difference spectra show a shift of 2 cm-1 to lower frequency of the band resulting from the absorbance of E286 in the oxidized enzyme. The decoupling mutants may influence E286 by altering the chain of water molecules which runs from the site of the mutations to E286.",

keywords = "Conformation, FTIR, Glutamate, Oxidase, Proton pump, Water",

author = "Vakkasoglu, {Ahmet S.} and Morgan, {Joel E.} and Dan Han and Pawate, {Ashtamurthy S.} and Gennis, {Robert B.}",

note = "Funding Information: This work was funded by a grant from the National Institutes of Health HL16101 (to R.B.G.), using instrumentation purchased using funds from a Critical Research Initiatives (CRI) Award from the University of Illinois. Authors thank Stuart Rose for writing the fluid flow control software.",

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doi = "10.1016/j.febslet.2006.07.036",

language = "English (US)",

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journal = "FEBS Letters",

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AU - Vakkasoglu, Ahmet S.

AU - Morgan, Joel E.

AU - Han, Dan

AU - Pawate, Ashtamurthy S.

AU - Gennis, Robert B.

N1 - Funding Information: This work was funded by a grant from the National Institutes of Health HL16101 (to R.B.G.), using instrumentation purchased using funds from a Critical Research Initiatives (CRI) Award from the University of Illinois. Authors thank Stuart Rose for writing the fluid flow control software.

PY - 2006/8/21

Y1 - 2006/8/21

N2 - Mutants that decouple the proton pump of cytochrome c oxidase from Rhodobacter sphaeroides are postulated to do so by increasing the pKa of glutamate 286, which is 20 Å away. The possibility that a conformational change near E286 is induced by the decoupling mutations (N139D and N207D) was investigated by FTIR difference spectroscopy. In both decoupled mutants, the reduced-minus-oxidized FTIR difference spectra show a shift of 2 cm-1 to lower frequency of the band resulting from the absorbance of E286 in the oxidized enzyme. The decoupling mutants may influence E286 by altering the chain of water molecules which runs from the site of the mutations to E286.

AB - Mutants that decouple the proton pump of cytochrome c oxidase from Rhodobacter sphaeroides are postulated to do so by increasing the pKa of glutamate 286, which is 20 Å away. The possibility that a conformational change near E286 is induced by the decoupling mutations (N139D and N207D) was investigated by FTIR difference spectroscopy. In both decoupled mutants, the reduced-minus-oxidized FTIR difference spectra show a shift of 2 cm-1 to lower frequency of the band resulting from the absorbance of E286 in the oxidized enzyme. The decoupling mutants may influence E286 by altering the chain of water molecules which runs from the site of the mutations to E286.

KW - Conformation

KW - FTIR

KW - Glutamate

KW - Oxidase

KW - Proton pump

KW - Water

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SN - 0014-5793

VL - 580

SP - 4613

EP - 4617

JO - FEBS Letters

JF - FEBS Letters

IS - 19

ER -

Mutations which decouple the proton pump of the cytochrome c oxidase from Rhodobacter sphaeroides perturb the environment of glutamate 286

Abstract

Keywords

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