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

^*Korrespondierende/r Autor/-in für diese Arbeit

9 Zitate (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.

Originalsprache	Englisch
Zeitschrift	Hyperfine Interactions
Jahrgang	156-157
Ausgabenummer	1-4
Seiten (von - bis)	293-298
Seitenumfang	6
ISSN	0304-3843
DOIs	https://doi.org/10.1023/B:HYPE.0000043243.81833.85
Publikationsstatus	Veröffentlicht - 01.03.2004

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10.1023/B:HYPE.0000043243.81833.85

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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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doi = "10.1023/B:HYPE.0000043243.81833.85",

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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 - http://www.scopus.com/inward/record.url?scp=33745408845&partnerID=8YFLogxK

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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