Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase

Victor S. Sharov; Deborah A. Ferrington; Thomas C. Squier; Christian Schöneich

doi:10.1016/S0014-5793(99)00888-1

Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase

Victor S. Sharov, Deborah A. Ferrington, Thomas C. Squier, Christian Schöneich

Ophthalmology & Visual Neurosciences

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

167 Scopus citations

Abstract

Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D-sulfoxide diastereomer of CaM-bound L-MetSO (L-Met-D-SO). After exhaustive reduction by pMSR, the ratio of L-Met-D-SO to L-Met-L-SO decreased to about 1:25 for hydrogen peroxide-oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR. Copyright (C) 1999 Federation of European Biochemical Societies.

Original language	English (US)
Pages (from-to)	247-250
Number of pages	4
Journal	FEBS Letters
Volume	455
Issue number	3
DOIs	https://doi.org/10.1016/S0014-5793(99)00888-1
State	Published - Jul 23 1999

Bibliographical note

Funding Information:
This study was supported by the National Institutes of Health (Grant P01AG12993). We thank Todd D. Williams of the KU Mass Spectrometry Laboratory for acquiring the ESI MS spectra, and Drs. J. Moskovitz and R.L. Levine for providing the pMSR clone.

Keywords

Calmodulin
Diastereoselectivity
Hydrogen peroxide
Methionine sulfoxide
Oxidative stress
Peptide methionine sulfoxide reductase

Access

10.1016/S0014-5793(99)00888-1

OpenUrl availability

Full text

Cite this

@article{7c4889d1d0de4f9390d99501a3386d58,

title = "Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase",

abstract = "Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D-sulfoxide diastereomer of CaM-bound L-MetSO (L-Met-D-SO). After exhaustive reduction by pMSR, the ratio of L-Met-D-SO to L-Met-L-SO decreased to about 1:25 for hydrogen peroxide-oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR. Copyright (C) 1999 Federation of European Biochemical Societies.",

keywords = "Calmodulin, Diastereoselectivity, Hydrogen peroxide, Methionine sulfoxide, Oxidative stress, Peptide methionine sulfoxide reductase",

author = "Sharov, {Victor S.} and Ferrington, {Deborah A.} and Squier, {Thomas C.} and Christian Sch{\"o}neich",

note = "Funding Information: This study was supported by the National Institutes of Health (Grant P01AG12993). We thank Todd D. Williams of the KU Mass Spectrometry Laboratory for acquiring the ESI MS spectra, and Drs. J. Moskovitz and R.L. Levine for providing the pMSR clone.",

year = "1999",

month = jul,

day = "23",

doi = "10.1016/S0014-5793(99)00888-1",

language = "English (US)",

volume = "455",

pages = "247--250",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "3",

}

TY - JOUR

T1 - Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase

AU - Sharov, Victor S.

AU - Ferrington, Deborah A.

AU - Squier, Thomas C.

AU - Schöneich, Christian

N1 - Funding Information: This study was supported by the National Institutes of Health (Grant P01AG12993). We thank Todd D. Williams of the KU Mass Spectrometry Laboratory for acquiring the ESI MS spectra, and Drs. J. Moskovitz and R.L. Levine for providing the pMSR clone.

PY - 1999/7/23

Y1 - 1999/7/23

N2 - Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D-sulfoxide diastereomer of CaM-bound L-MetSO (L-Met-D-SO). After exhaustive reduction by pMSR, the ratio of L-Met-D-SO to L-Met-L-SO decreased to about 1:25 for hydrogen peroxide-oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR. Copyright (C) 1999 Federation of European Biochemical Societies.

AB - Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D-sulfoxide diastereomer of CaM-bound L-MetSO (L-Met-D-SO). After exhaustive reduction by pMSR, the ratio of L-Met-D-SO to L-Met-L-SO decreased to about 1:25 for hydrogen peroxide-oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR. Copyright (C) 1999 Federation of European Biochemical Societies.

KW - Calmodulin

KW - Diastereoselectivity

KW - Hydrogen peroxide

KW - Methionine sulfoxide

KW - Oxidative stress

KW - Peptide methionine sulfoxide reductase

UR - http://www.scopus.com/inward/record.url?scp=0032815727&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032815727&partnerID=8YFLogxK

U2 - 10.1016/S0014-5793(99)00888-1

DO - 10.1016/S0014-5793(99)00888-1

M3 - Article

C2 - 10437782

AN - SCOPUS:0032815727

SN - 0014-5793

VL - 455

SP - 247

EP - 250

JO - FEBS Letters

JF - FEBS Letters

IS - 3

ER -

Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase

Abstract

Bibliographical note

Keywords

Access

OpenUrl availability

Other files and links

Fingerprint

Cite this