Transfer of sulfur to biotin from biotin synthase (BioB protein)

Katharine J. Gibson; Dale A. Pelletier; Ivan M. Turner

doi:10.1006/bbrc.1998.9991

Transfer of sulfur to biotin from biotin synthase (BioB protein)

Katharine J. Gibson
, Dale A. Pelletier
, Ivan M. Turner

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

63 Scopus citations

Abstract

In biotin synthase reactions carried out in vitro, we observed efficient transfer of ³⁵S to biotin from partially purified E. coli biotin synthase (product of the bioB gene) labelled by biosynthetic incorporation of [³⁵S]-cysteine. Mass spectrometry was consistent with covalent alteration of the protein in the assay. These results suggest that BioB protein is a reagent, not a catalyst.

Original language	English
Pages (from-to)	632-635
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	254
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1998.9991
State	Published - Jan 27 1999
Externally published	Yes

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title = "Transfer of sulfur to biotin from biotin synthase (BioB protein)",

abstract = "In biotin synthase reactions carried out in vitro, we observed efficient transfer of 35S to biotin from partially purified E. coli biotin synthase (product of the bioB gene) labelled by biosynthetic incorporation of [35S]-cysteine. Mass spectrometry was consistent with covalent alteration of the protein in the assay. These results suggest that BioB protein is a reagent, not a catalyst.",

author = "Gibson, \{Katharine J.\} and Pelletier, \{Dale A.\} and Turner, \{Ivan M.\}",

year = "1999",

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doi = "10.1006/bbrc.1998.9991",

language = "English",

volume = "254",

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journal = "Biochemical and Biophysical Research Communications",

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T1 - Transfer of sulfur to biotin from biotin synthase (BioB protein)

AU - Gibson, Katharine J.

AU - Pelletier, Dale A.

AU - Turner, Ivan M.

PY - 1999/1/27

Y1 - 1999/1/27

N2 - In biotin synthase reactions carried out in vitro, we observed efficient transfer of 35S to biotin from partially purified E. coli biotin synthase (product of the bioB gene) labelled by biosynthetic incorporation of [35S]-cysteine. Mass spectrometry was consistent with covalent alteration of the protein in the assay. These results suggest that BioB protein is a reagent, not a catalyst.

AB - In biotin synthase reactions carried out in vitro, we observed efficient transfer of 35S to biotin from partially purified E. coli biotin synthase (product of the bioB gene) labelled by biosynthetic incorporation of [35S]-cysteine. Mass spectrometry was consistent with covalent alteration of the protein in the assay. These results suggest that BioB protein is a reagent, not a catalyst.

UR - https://www.scopus.com/pages/publications/0033608163

U2 - 10.1006/bbrc.1998.9991

DO - 10.1006/bbrc.1998.9991

M3 - Article

C2 - 9920791

AN - SCOPUS:0033608163

SN - 0006-291X

VL - 254

SP - 632

EP - 635

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Transfer of sulfur to biotin from biotin synthase (BioB protein)

Abstract

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