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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| Format: | Article |
| Language: | English |
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Hindawi Publishing Corporation
2014
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| Online Access: | http://psasir.upm.edu.my/id/eprint/34589/ http://psasir.upm.edu.my/id/eprint/34589/1/Molybdenum%20Reduction%20to%20Molybdenum.pdf |
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| author | Abd. Shukor, Mohd. Yunus Halmi, Mohd Izuan Effendi Abd. Rahman, Mohd Fadhil Shamaan, Nor Aripin Syed, Mohd Arif |
| 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 |
| building | UPM Institutional Repository |
| collection | Online Access |
| 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. |
| first_indexed | 2025-11-15T09:24:37Z |
| format | Article |
| id | upm-34589 |
| institution | Universiti Putra Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T09:24:37Z |
| publishDate | 2014 |
| publisher | Hindawi Publishing Corporation |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | upm-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 |
| 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 |
| title | 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_short | 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 |
| url | http://psasir.upm.edu.my/id/eprint/34589/ http://psasir.upm.edu.my/id/eprint/34589/ http://psasir.upm.edu.my/id/eprint/34589/ http://psasir.upm.edu.my/id/eprint/34589/1/Molybdenum%20Reduction%20to%20Molybdenum.pdf |