The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre
Yeast Erv1p is a ubiquitous FAD-dependent sulfhydryl oxidase, located in the intermembrane space of mitochondria. The dimeric enzyme is essential for survival of the cell. Besides the redox-active CXXC motif close to the FAD, Erv1p harbours two additional cysteine pairs. Site-directed mutagenesis has identified all three cysteine pairs as essential for normal function. The C-terminal cysteine pair is of structural importance as it contributes to the correct arrangement of the FAD-binding fold. Variations in dimer formation and unique colour changes of mutant proteins argue in favour of an interaction between the N-terminal cysteine pair with the redox centre of the partner monomer.
Cysteine mutants, Dimer formation, Mitochondrial Erv1p, Redox-active CXXC, Sulfhydryl oxidase
1528-1535
Hofhaus, Götz
af06014d-47fe-405c-a802-e6df39fe5381
Lee, Jeung Eun
d7b239cc-0fd3-4a6c-bc72-be23d8e14a0e
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Rosenberg, Beate
f7f1f6f4-a654-4a18-92f8-308a830f26d5
Lisowsky, Thomas
dfc93739-2dfa-4876-b3fc-327df1f4c1c3
April 2003
Hofhaus, Götz
af06014d-47fe-405c-a802-e6df39fe5381
Lee, Jeung Eun
d7b239cc-0fd3-4a6c-bc72-be23d8e14a0e
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Rosenberg, Beate
f7f1f6f4-a654-4a18-92f8-308a830f26d5
Lisowsky, Thomas
dfc93739-2dfa-4876-b3fc-327df1f4c1c3
Hofhaus, Götz, Lee, Jeung Eun, Tews, Ivo, Rosenberg, Beate and Lisowsky, Thomas
(2003)
The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre.
European Journal of Biochemistry, 270 (7), .
(doi:10.1046/j.1432-1033.2003.03519.x).
Abstract
Yeast Erv1p is a ubiquitous FAD-dependent sulfhydryl oxidase, located in the intermembrane space of mitochondria. The dimeric enzyme is essential for survival of the cell. Besides the redox-active CXXC motif close to the FAD, Erv1p harbours two additional cysteine pairs. Site-directed mutagenesis has identified all three cysteine pairs as essential for normal function. The C-terminal cysteine pair is of structural importance as it contributes to the correct arrangement of the FAD-binding fold. Variations in dimer formation and unique colour changes of mutant proteins argue in favour of an interaction between the N-terminal cysteine pair with the redox centre of the partner monomer.
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e-pub ahead of print date: 17 March 2003
Published date: April 2003
Keywords:
Cysteine mutants, Dimer formation, Mitochondrial Erv1p, Redox-active CXXC, Sulfhydryl oxidase
Identifiers
Local EPrints ID: 500527
URI: http://eprints.soton.ac.uk/id/eprint/500527
ISSN: 0014-2956
PURE UUID: 33e3a005-86d4-4bba-8ca5-654cf6a571c5
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Date deposited: 02 May 2025 16:59
Last modified: 03 May 2025 01:45
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Contributors
Author:
Götz Hofhaus
Author:
Jeung Eun Lee
Author:
Beate Rosenberg
Author:
Thomas Lisowsky
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