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

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dc.Chemicals/CASmolybdenum, 7439-98-7; reduced nicotinamide adenine dinucleotide, 58-68-4; oxidoreductase, 9035-73-8, 9035-82-9, 9037-80-3, 9055-15-6; Bacterial Proteins; Molybdenum; Oxidoreductases
dc.citedby18
dc.contributor.affiliationsFaculty of Medicine and Health Sciences
dc.contributor.affiliationsUniversiti Putra Malaysia (UPM)
dc.contributor.affiliationsUniversiti Sains Islam Malaysia (USIM)
dc.contributor.authorShukor M.Y.en_US
dc.contributor.authorHalmi M.I.E.en_US
dc.contributor.authorRahman M.F.A.en_US
dc.contributor.authorShamaan N.A.en_US
dc.contributor.authorSyed M.A.en_US
dc.date.accessioned2024-05-29T01:56:37Z
dc.date.available2024-05-29T01:56:37Z
dc.date.issued2014
dc.description.abstractThe 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 V m a x for NADH at 12.0 nmole Mo blue/min/mg protein. The apparent K m for NADH was 0.79 mM. At 5 mM NADH, the apparent V m a x and apparent K m values for 12-MP of 12.05 nmole/min/mg protein and 3.87 mM, respectively, were obtained. The catalytic efficiency (k c a t / K m) of the Mo-reducing enzyme was 5.47 M - 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.en_US
dc.description.natureFinalen_US
dc.identifier.ArtNo853084
dc.identifier.doi10.1155/2014/853084
dc.identifier.issn23146133
dc.identifier.pmid24724104
dc.identifier.scopus2-s2.0-84897900479
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84897900479&doi=10.1155%2f2014%2f853084&partnerID=40&md5=ebe35974c0e4de347e1c176cf39568ce
dc.identifier.urihttps://oarep.usim.edu.my/handle/123456789/9856
dc.identifier.volume2014
dc.languageEnglish
dc.language.isoen_USen_US
dc.publisherHindawi Publishing Corporationen_US
dc.relation.ispartofOpen Accessen_US
dc.relation.ispartofBioMed Research International
dc.sourceScopus
dc.titleMolybdenum reduction to molybdenum blue in Serratia sp. strain DRY5 is catalyzed by a novel molybdenum-reducing enzymeen_US
dc.title.alternativeBioMed Res. Int.en_US
dc.typeArticleen_US
dspace.entity.typePublication

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