Detergent-solubilized Escherichia coli cytochrome bo3 ubiquinol oxidase: A monomeric, not a dimeric complex

Andrej Musatov; Jaime Ortega-Lopez; Borries Demeler; Jeffrey P. Osborne; Robert B. Gennis; Neal C. Robinson

doi:10.1016/S0014-5793(99)01020-0

Detergent-solubilized Escherichia coli cytochrome bo₃ ubiquinol oxidase: A monomeric, not a dimeric complex

Andrej Musatov, Jaime Ortega-Lopez, Borries Demeler, Jeffrey P. Osborne, Robert B. Gennis, Neal C. Robinson

Chemistry

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

14 Scopus citations

Abstract

The protein molecular weight, M(r), and hydrodynamic radius, R(s), of Triton X-100-solubilized Escherichia coli cytochrome bo₃ were evaluated by computer fitting of sedimentation velocity data with finite element solutions to the Lamm equation. Detergent-solubilized cytochrome bo₃ sediments as a homogeneous species with an s(20,w) of 6.75 s and a D(20,w) of 3.71x10^-7 cm²/s, corresponding to a R(s) of 5.8 nm and a M(r) of 144 000±3500. The protein molecular weight agrees very well with the value of 143 929 calculated from the four known subunit sequences and the value of 143 025 measured by MALDI mass spectrometry for the histidine-tagged enzyme. We conclude that detergent-solubilized E. coli ubiquinol oxidase is a monomeric complex of the four known subunits. Copyright (C) 1999 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	153-156
Number of pages	4
Journal	FEBS Letters
Volume	457
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(99)01020-0
State	Published - Aug 20 1999

Keywords

Computer analysis
Cytochrome bo ubiquinol oxidase
Escherichia coli
Sedimentation equilibrium
Sedimentation velocity

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10.1016/S0014-5793(99)01020-0

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@article{ec85222fc14f484cbc596c2817a5875c,

title = "Detergent-solubilized Escherichia coli cytochrome bo3 ubiquinol oxidase: A monomeric, not a dimeric complex",

abstract = "The protein molecular weight, M(r), and hydrodynamic radius, R(s), of Triton X-100-solubilized Escherichia coli cytochrome bo3 were evaluated by computer fitting of sedimentation velocity data with finite element solutions to the Lamm equation. Detergent-solubilized cytochrome bo3 sediments as a homogeneous species with an s(20,w) of 6.75 s and a D(20,w) of 3.71x10-7 cm2/s, corresponding to a R(s) of 5.8 nm and a M(r) of 144 000±3500. The protein molecular weight agrees very well with the value of 143 929 calculated from the four known subunit sequences and the value of 143 025 measured by MALDI mass spectrometry for the histidine-tagged enzyme. We conclude that detergent-solubilized E. coli ubiquinol oxidase is a monomeric complex of the four known subunits. Copyright (C) 1999 Federation of European Biochemical Societies.",

keywords = "Computer analysis, Cytochrome bo ubiquinol oxidase, Escherichia coli, Sedimentation equilibrium, Sedimentation velocity",

author = "Andrej Musatov and Jaime Ortega-Lopez and Borries Demeler and Osborne, {Jeffrey P.} and Gennis, {Robert B.} and Robinson, {Neal C.}",

note = "Funding Information: This work was supported by research Grants to NCR from the National Institute of General Medical Science (GM 24795) and to RBG from the Dept. of Energy (DEFG02-87ER13716).",

year = "1999",

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doi = "10.1016/S0014-5793(99)01020-0",

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T1 - Detergent-solubilized Escherichia coli cytochrome bo3 ubiquinol oxidase

T2 - A monomeric, not a dimeric complex

AU - Musatov, Andrej

AU - Ortega-Lopez, Jaime

AU - Demeler, Borries

AU - Osborne, Jeffrey P.

AU - Gennis, Robert B.

AU - Robinson, Neal C.

N1 - Funding Information: This work was supported by research Grants to NCR from the National Institute of General Medical Science (GM 24795) and to RBG from the Dept. of Energy (DEFG02-87ER13716).

PY - 1999/8/20

Y1 - 1999/8/20

N2 - The protein molecular weight, M(r), and hydrodynamic radius, R(s), of Triton X-100-solubilized Escherichia coli cytochrome bo3 were evaluated by computer fitting of sedimentation velocity data with finite element solutions to the Lamm equation. Detergent-solubilized cytochrome bo3 sediments as a homogeneous species with an s(20,w) of 6.75 s and a D(20,w) of 3.71x10-7 cm2/s, corresponding to a R(s) of 5.8 nm and a M(r) of 144 000±3500. The protein molecular weight agrees very well with the value of 143 929 calculated from the four known subunit sequences and the value of 143 025 measured by MALDI mass spectrometry for the histidine-tagged enzyme. We conclude that detergent-solubilized E. coli ubiquinol oxidase is a monomeric complex of the four known subunits. Copyright (C) 1999 Federation of European Biochemical Societies.

AB - The protein molecular weight, M(r), and hydrodynamic radius, R(s), of Triton X-100-solubilized Escherichia coli cytochrome bo3 were evaluated by computer fitting of sedimentation velocity data with finite element solutions to the Lamm equation. Detergent-solubilized cytochrome bo3 sediments as a homogeneous species with an s(20,w) of 6.75 s and a D(20,w) of 3.71x10-7 cm2/s, corresponding to a R(s) of 5.8 nm and a M(r) of 144 000±3500. The protein molecular weight agrees very well with the value of 143 929 calculated from the four known subunit sequences and the value of 143 025 measured by MALDI mass spectrometry for the histidine-tagged enzyme. We conclude that detergent-solubilized E. coli ubiquinol oxidase is a monomeric complex of the four known subunits. Copyright (C) 1999 Federation of European Biochemical Societies.

KW - Computer analysis

KW - Cytochrome bo ubiquinol oxidase

KW - Escherichia coli

KW - Sedimentation equilibrium

KW - Sedimentation velocity

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U2 - 10.1016/S0014-5793(99)01020-0

DO - 10.1016/S0014-5793(99)01020-0

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AN - SCOPUS:0032765698

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JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

Detergent-solubilized Escherichia coli cytochrome bo₃ ubiquinol oxidase: A monomeric, not a dimeric complex

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