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

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

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Abstract

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.

Item Type:Article
Keyword:Molybdenum reduction; Molybdenum blue; Serratia sp. strain DRY5
Faculty or Institute:Faculty of Biotechnology and Biomolecular Sciences
Publisher:Hindawi Publishing Corporation
DOI Number:10.1155/2014/853084
Altmetrics:http://www.altmetric.com/details.php?domain=psasir.upm.edu.my&doi=10.1155/2014/853084
ID Code:34589
Deposited By: Nurul Ainie Mokhtar
Deposited On:16 Dec 2015 11:14
Last Modified:21 Apr 2017 09:34

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