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Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme

The first purification of the Mo-reducing enzyme from Serratia sp. strain DRY5 that is responsible for molybdenum reduction to molybdenum blue in the bacterium is reported. The monomeric enzyme has an apparent molecular weight of 105 kDalton. The isoelectric point of this enzyme was 7.55. The enzyme...

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Main Authors: Abd. Shukor, Mohd. Yunus, Halmi, Mohd Izuan Effendi, Abd. Rahman, Mohd Fadhil, Shamaan, Nor Aripin, Syed, Mohd Arif
Format: Article
Language:English
Published: Hindawi Publishing Corporation 2014
Online Access:http://psasir.upm.edu.my/id/eprint/34589/1/Molybdenum%20Reduction%20to%20Molybdenum.pdf
http://psasir.upm.edu.my/id/eprint/34589/
http://www.hindawi.com/journals/bmri/2014/853084/abs/
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spelling my.upm.eprints.345892017-04-21T01:34:36Z http://psasir.upm.edu.my/id/eprint/34589/ Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme Abd. Shukor, Mohd. Yunus Halmi, Mohd Izuan Effendi Abd. Rahman, Mohd Fadhil Shamaan, Nor Aripin Syed, Mohd Arif The first purification of the Mo-reducing enzyme from Serratia sp. strain DRY5 that is responsible for molybdenum reduction to molybdenum blue in the bacterium is reported. The monomeric enzyme has an apparent molecular weight of 105 kDalton. The isoelectric point of this enzyme was 7.55. The enzyme has an optimum pH of 6.0 and maximum activity between 25 and 35°C. The Mo-reducing enzyme was extremely sensitive to temperatures above 50°C (between 54 and 70°C). A plot of initial rates against substrate concentrations at 15 mM 12-MP registered a for NADH at 12.0 nmole Mo blue/min/mg protein. The apparent for NADH was 0.79 mM. At 5 mM NADH, the apparent and apparent values for 12-MP of 12.05 nmole/min/mg protein and 3.87 mM, respectively, were obtained. The catalytic efficiency ( / ) of the Mo-reducing enzyme was 5.47  . The purification of this enzyme could probably help to solve the phenomenon of molybdenum reduction to molybdenum blue first reported in 1896 and would be useful for the understanding of the underlying mechanism in molybdenum bioremediation involving bioreduction. Hindawi Publishing Corporation 2014 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/34589/1/Molybdenum%20Reduction%20to%20Molybdenum.pdf Abd. Shukor, Mohd. Yunus and Halmi, Mohd Izuan Effendi and Abd. Rahman, Mohd Fadhil and Shamaan, Nor Aripin and Syed, Mohd Arif (2014) Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme. BioMed Research International, 2014. art. no. 853084. pp. 1-8. ISSN 2314-6133; ESSN: 2314-6141 http://www.hindawi.com/journals/bmri/2014/853084/abs/ 10.1155/2014/853084
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description The first purification of the Mo-reducing enzyme from Serratia sp. strain DRY5 that is responsible for molybdenum reduction to molybdenum blue in the bacterium is reported. The monomeric enzyme has an apparent molecular weight of 105 kDalton. The isoelectric point of this enzyme was 7.55. The enzyme has an optimum pH of 6.0 and maximum activity between 25 and 35°C. The Mo-reducing enzyme was extremely sensitive to temperatures above 50°C (between 54 and 70°C). A plot of initial rates against substrate concentrations at 15 mM 12-MP registered a for NADH at 12.0 nmole Mo blue/min/mg protein. The apparent for NADH was 0.79 mM. At 5 mM NADH, the apparent and apparent values for 12-MP of 12.05 nmole/min/mg protein and 3.87 mM, respectively, were obtained. The catalytic efficiency ( / ) of the Mo-reducing enzyme was 5.47  . The purification of this enzyme could probably help to solve the phenomenon of molybdenum reduction to molybdenum blue first reported in 1896 and would be useful for the understanding of the underlying mechanism in molybdenum bioremediation involving bioreduction.
format Article
author Abd. Shukor, Mohd. Yunus
Halmi, Mohd Izuan Effendi
Abd. Rahman, Mohd Fadhil
Shamaan, Nor Aripin
Syed, Mohd Arif
spellingShingle Abd. Shukor, Mohd. Yunus
Halmi, Mohd Izuan Effendi
Abd. Rahman, Mohd Fadhil
Shamaan, Nor Aripin
Syed, Mohd Arif
Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme
author_facet Abd. Shukor, Mohd. Yunus
Halmi, Mohd Izuan Effendi
Abd. Rahman, Mohd Fadhil
Shamaan, Nor Aripin
Syed, Mohd Arif
author_sort Abd. Shukor, Mohd. Yunus
title Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme
title_short Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme
title_full Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme
title_fullStr Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme
title_full_unstemmed Molybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzyme
title_sort molybdenum reduction to molybdenum blue in serratia sp. strain dry5 is catalyzed by a novel molybdenum-reducing enzyme
publisher Hindawi Publishing Corporation
publishDate 2014
url http://psasir.upm.edu.my/id/eprint/34589/1/Molybdenum%20Reduction%20to%20Molybdenum.pdf
http://psasir.upm.edu.my/id/eprint/34589/
http://www.hindawi.com/journals/bmri/2014/853084/abs/
_version_ 1643831199529959424
score 13.211869

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