Mössbauer characterization of the Fe-S center in the catalytic metal binding site of alcohol dehydrogenase

C. Haas; H. Dietrich; W. Maret; M. Zeppezauer; R. Montiel-Montoya; E. Bill; A. X. Trautwein

doi:10.1007/BF02399500

Mössbauer characterization of the Fe-S center in the catalytic metal binding site of alcohol dehydrogenase

C. Haas^*, H. Dietrich, W. Maret, M. Zeppezauer, R. Montiel-Montoya, E. Bill, A. X. Trautwein

^*Corresponding author for this work

4 Citations (Scopus)

Abstract

Iron in its divalent and trivalent form can be substituted in the catalytic zinc site of alcohol dehydrogenase from horse liver (HLADH). Fe-HLADH in either oxidation state does not show enzymatic activity in the oxidation of ethanol. Nevertheless, Mössbauer studies of this material are of considerable interest, because they elucidate the effect of pH and coenzyme-induced conformational changes of the protein on the metal ion. It is of importance to note that zinc itself due to the lack of suitable chromophoric and magnetic properties does not provide any comparable information.

Original language	English
Journal	Hyperfine Interactions
Volume	29
Issue number	1-4
Pages (from-to)	1419-1422
Number of pages	4
ISSN	0304-3843
DOIs	https://doi.org/10.1007/BF02399500
Publication status	Published - 01.02.1986

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title = "M{\"o}ssbauer characterization of the Fe-S center in the catalytic metal binding site of alcohol dehydrogenase",

abstract = "Iron in its divalent and trivalent form can be substituted in the catalytic zinc site of alcohol dehydrogenase from horse liver (HLADH). Fe-HLADH in either oxidation state does not show enzymatic activity in the oxidation of ethanol. Nevertheless, M{\"o}ssbauer studies of this material are of considerable interest, because they elucidate the effect of pH and coenzyme-induced conformational changes of the protein on the metal ion. It is of importance to note that zinc itself due to the lack of suitable chromophoric and magnetic properties does not provide any comparable information.",

author = "C. Haas and H. Dietrich and W. Maret and M. Zeppezauer and R. Montiel-Montoya and E. Bill and Trautwein, {A. X.}",

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T1 - Mössbauer characterization of the Fe-S center in the catalytic metal binding site of alcohol dehydrogenase

AU - Haas, C.

AU - Dietrich, H.

AU - Maret, W.

AU - Zeppezauer, M.

AU - Montiel-Montoya, R.

AU - Bill, E.

AU - Trautwein, A. X.

PY - 1986/2/1

Y1 - 1986/2/1

N2 - Iron in its divalent and trivalent form can be substituted in the catalytic zinc site of alcohol dehydrogenase from horse liver (HLADH). Fe-HLADH in either oxidation state does not show enzymatic activity in the oxidation of ethanol. Nevertheless, Mössbauer studies of this material are of considerable interest, because they elucidate the effect of pH and coenzyme-induced conformational changes of the protein on the metal ion. It is of importance to note that zinc itself due to the lack of suitable chromophoric and magnetic properties does not provide any comparable information.

AB - Iron in its divalent and trivalent form can be substituted in the catalytic zinc site of alcohol dehydrogenase from horse liver (HLADH). Fe-HLADH in either oxidation state does not show enzymatic activity in the oxidation of ethanol. Nevertheless, Mössbauer studies of this material are of considerable interest, because they elucidate the effect of pH and coenzyme-induced conformational changes of the protein on the metal ion. It is of importance to note that zinc itself due to the lack of suitable chromophoric and magnetic properties does not provide any comparable information.

UR - http://www.scopus.com/inward/record.url?scp=34250125075&partnerID=8YFLogxK

U2 - 10.1007/BF02399500

DO - 10.1007/BF02399500

M3 - Journal articles

AN - SCOPUS:34250125075

SN - 0304-3843

VL - 29

SP - 1419

EP - 1422

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 1-4

ER -

Mössbauer characterization of the Fe-S center in the catalytic metal binding site of alcohol dehydrogenase

Abstract

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