Iron-sulfur proteins investigated by EPR-, Mössbauer- and EXAFS-spectroscopy

P. Wegner; M. Bever; V. Schünemann; A. X. Trautwein; C. Schmidt; H. Bönisch; M. Gnida; W. Meyer-Klaucke

doi:10.1023/B:HYPE.0000043243.81833.85

Iron-sulfur proteins investigated by EPR-, Mössbauer- and EXAFS-spectroscopy

P. Wegner^*, M. Bever, V. Schünemann, A. X. Trautwein, C. Schmidt, H. Bönisch, M. Gnida, W. Meyer-Klaucke

^*Corresponding author for this work

12 Citations (Scopus)

Abstract

The structural and spectroscopic properties of the biologically active [Fe-4S] site of three different mutants of the wild-type rubredoxin from the archaeon Pyrococcus abyssi were investigated and compared with each other and additionally with those of the rubredoxin from the bacterium Clostridium pasteurianum.

Original language	English
Journal	Hyperfine Interactions
Volume	156-157
Issue number	1-4
Pages (from-to)	293-298
Number of pages	6
ISSN	0304-3843
DOIs	https://doi.org/10.1023/B:HYPE.0000043243.81833.85
Publication status	Published - 01.03.2004

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10.1023/B:HYPE.0000043243.81833.85

Cite this

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title = "Iron-sulfur proteins investigated by EPR-, M{\"o}ssbauer- and EXAFS-spectroscopy",

abstract = "The structural and spectroscopic properties of the biologically active [Fe-4S] site of three different mutants of the wild-type rubredoxin from the archaeon Pyrococcus abyssi were investigated and compared with each other and additionally with those of the rubredoxin from the bacterium Clostridium pasteurianum.",

author = "P. Wegner and M. Bever and V. Sch{\"u}nemann and Trautwein, \{A. X.\} and C. Schmidt and H. B{\"o}nisch and M. Gnida and W. Meyer-Klaucke",

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T1 - Iron-sulfur proteins investigated by EPR-, Mössbauer- and EXAFS-spectroscopy

AU - Wegner, P.

AU - Bever, M.

AU - Schünemann, V.

AU - Trautwein, A. X.

AU - Schmidt, C.

AU - Bönisch, H.

AU - Gnida, M.

AU - Meyer-Klaucke, W.

PY - 2004/3/1

Y1 - 2004/3/1

N2 - The structural and spectroscopic properties of the biologically active [Fe-4S] site of three different mutants of the wild-type rubredoxin from the archaeon Pyrococcus abyssi were investigated and compared with each other and additionally with those of the rubredoxin from the bacterium Clostridium pasteurianum.

AB - The structural and spectroscopic properties of the biologically active [Fe-4S] site of three different mutants of the wild-type rubredoxin from the archaeon Pyrococcus abyssi were investigated and compared with each other and additionally with those of the rubredoxin from the bacterium Clostridium pasteurianum.

UR - https://www.scopus.com/pages/publications/33745408845

U2 - 10.1023/B:HYPE.0000043243.81833.85

DO - 10.1023/B:HYPE.0000043243.81833.85

M3 - Journal articles

AN - SCOPUS:33745408845

SN - 0304-3843

VL - 156-157

SP - 293

EP - 298

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Iron-sulfur proteins investigated by EPR-, Mössbauer- and EXAFS-spectroscopy

Abstract

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