Staff View: Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme

Molybdate 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:	M. Y, Shukor,, M. I. E., Halmi,, M. F. A., Rahman,, M. A., Syed,, N. A., Shamaan,
Format:	Article
Language:	en_US
Published:	Hindawi Publishing Corporation 2015
Subjects:	Thiobacillus-Ferrooxidans Hexavalent Molybdenum Enterobacter-Cloacae Molybdate Reduction Bacterium Ion
Online Access:	http://www.hindawi.com/journals/bmri/2014/853084/
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spelling	my.usim-84692015-12-29T03:06:42Z Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme M. Y, Shukor, M. I. E., Halmi, M. F. A., Rahman, M. A., Syed, N. A., Shamaan, Thiobacillus-Ferrooxidans Hexavalent Molybdenum Enterobacter-Cloacae Molybdate Reduction Bacterium Ion 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 degrees C. The Mo-reducing enzyme was extremely sensitive to temperatures above 50 degrees C (between 54 and 70 degrees C). A plot of initial rates against substrate concentrations at 15mM 12-MP registered a V-max for NADH at 12.0 nmole Mo blue/min/mg protein. The apparent k(m) for NADH was 0.79mM. At 5mM NADH, the apparent V-max and apparent k(m) values for 12-MP of 12.05 nmole/min/mg protein and 3.87mM, respectively, were obtained. The catalytic efficiency (k(cat)/k(m)) of the Mo-reducing enzyme was 5.47M(-1) s(-1). 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. 2015-06-22T02:12:02Z 2015-06-22T02:12:02Z 2014-01-01 Article 2314-6133 2314-6141 http://www.hindawi.com/journals/bmri/2014/853084/ en_US Hindawi Publishing Corporation
institution	Universiti Sains Islam Malaysia
building	USIM Library
collection	Institutional Repository
continent	Asia
country	Malaysia
content_provider	Universit Sains Islam i Malaysia
content_source	USIM Institutional Repository
url_provider	http://ddms.usim.edu.my/
language	en_US
topic	Thiobacillus-Ferrooxidans Hexavalent Molybdenum Enterobacter-Cloacae Molybdate Reduction Bacterium Ion
spellingShingle	Thiobacillus-Ferrooxidans Hexavalent Molybdenum Enterobacter-Cloacae Molybdate Reduction Bacterium Ion M. Y, Shukor, M. I. E., Halmi, M. F. A., Rahman, M. A., Syed, N. A., Shamaan, Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme
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 degrees C. The Mo-reducing enzyme was extremely sensitive to temperatures above 50 degrees C (between 54 and 70 degrees C). A plot of initial rates against substrate concentrations at 15mM 12-MP registered a V-max for NADH at 12.0 nmole Mo blue/min/mg protein. The apparent k(m) for NADH was 0.79mM. At 5mM NADH, the apparent V-max and apparent k(m) values for 12-MP of 12.05 nmole/min/mg protein and 3.87mM, respectively, were obtained. The catalytic efficiency (k(cat)/k(m)) of the Mo-reducing enzyme was 5.47M(-1) s(-1). 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	M. Y, Shukor, M. I. E., Halmi, M. F. A., Rahman, M. A., Syed, N. A., Shamaan,
author_facet	M. Y, Shukor, M. I. E., Halmi, M. F. A., Rahman, M. A., Syed, N. A., Shamaan,
author_sort	M. Y, Shukor,
title	Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme
title_short	Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme
title_full	Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme
title_fullStr	Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme
title_full_unstemmed	Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme
title_sort	molybdate reduction to molybdenum blue in serratia sp strain dry5 is catalyzed by a novel molybdenum-reducing enzyme
publisher	Hindawi Publishing Corporation
publishDate	2015
url	http://www.hindawi.com/journals/bmri/2014/853084/
_version_	1645152423472267264
score	13.211869

Molybdate Reduction to Molybdenum Blue in Serratia sp Strain DRY5 Is Catalyzed by a Novel Molybdenum-Reducing Enzyme

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