Spectroscopic Changes during a Single Turnover of Biotin Synthase:  Destruction of a [2Fe-2S] Cluster Accompanies Sulfur Insertion†

Natalia B. Ugulava; Carlos J. Sacanell; Joseph T. Jarrett

doi:10.1021/bi010463x

Spectroscopic Changes during a Single Turnover of Biotin Synthase: Destruction of a [2Fe-2S] Cluster Accompanies Sulfur Insertion†

Biochemistry ◽

10.1021/bi010463x ◽

2001 ◽

Vol 40 (28) ◽

pp. 8352-8358 ◽

Cited By ~ 99

Author(s):

Natalia B. Ugulava ◽

Carlos J. Sacanell ◽

Joseph T. Jarrett

Keyword(s):

Biotin Synthase ◽

Single Turnover

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Faculty Opinions recommendation of Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1000360.7601 ◽

2001 ◽

Author(s):

Mark Nelson

Keyword(s):

Biotin Synthase ◽

Single Turnover

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Faculty Opinions recommendation of Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertion.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1000360.9763 ◽

2001 ◽

Author(s):

Marc Fontecave

Keyword(s):

Biotin Synthase ◽

Single Turnover

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Expression of genes encoding acetyl-CoA carboxylase, biotin synthase, and acetyl-CoA generating enzymes in Arabidopsis thaliana

10.31274/rtd-180813-13275 ◽

1997 ◽

Author(s):

Jinshan Ke

Keyword(s):

Arabidopsis Thaliana ◽

Acetyl Coa Carboxylase ◽

Acetyl Coa ◽

Biotin Synthase ◽

Expression Of Genes ◽

Genes Encoding

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Faculty Opinions recommendation of Biotin synthase is a pyridoxal phosphate-dependent cysteine desulfurase.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1007891.98205 ◽

2002 ◽

Author(s):

Ruma Banerjee

Keyword(s):

Pyridoxal Phosphate ◽

Cysteine Desulfurase ◽

Biotin Synthase

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Faculty Opinions recommendation of Escherichia coli biotin synthase produces selenobiotin. Further evidence of the involvement of the [2Fe-2S]2+ cluster in the sulfur insertion step.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1012077.367715 ◽

2006 ◽

Author(s):

Wolfgang Buckel

Keyword(s):

Escherichia Coli ◽

Biotin Synthase

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Faculty Opinions recommendation of Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1017429.203119 ◽

2004 ◽

Author(s):

Joan Broderick

Keyword(s):

Escherichia Coli ◽

Recombinant Escherichia Coli ◽

Biotin Synthase

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Single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)35424-9 ◽

1988 ◽

Vol 263 (2) ◽

pp. 791-798

Author(s):

C B Brewer ◽

J A Peterson

Keyword(s):

Single Turnover ◽

Kinetics Of

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Movement of the Iron-Sulfur Subunit beyond theefLoop of CytochromebIs Required for Multiple Turnovers of thebc1Complex but Not for Single Turnover QoSite Catalysis

Journal of Biological Chemistry ◽

10.1074/jbc.m107974200 ◽

2001 ◽

Vol 277 (5) ◽

pp. 3471-3476 ◽

Cited By ~ 45

Author(s):

Elisabeth Darrouzet ◽

Fevzi Daldal

Keyword(s):

Single Turnover ◽

Iron Sulfur

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ChemInform Abstract: The Insertion of Sulfur into the Non-Activated C-H Bond. A Possible Model for Penicillin Cyclase and Biotin Synthase.

ChemInform ◽

10.1002/chin.199209105 ◽

2010 ◽

Vol 23 (9) ◽

pp. no-no

Author(s):

G. BALAVOINE ◽

D. H. R. BARTON ◽

A. GREF ◽

I. LELLOUCHE

Keyword(s):

Biotin Synthase

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Structure-Function Studies of Escherichia coli Biotin Synthase via a Chemical Modification and Site-Directed Mutagenesis Approach

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a003028 ◽

2001 ◽

Vol 130 (5) ◽

pp. 627-635 ◽

Cited By ~ 7

Author(s):

L. Farh ◽

S.-Y. Hwang ◽

L. Steinrauf ◽

H.-J. Chiang ◽

D. Shiuan

Keyword(s):

Escherichia Coli ◽

Chemical Modification ◽

Structure Function ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Biotin Synthase

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