01934nas a2200229   4500008004100000022001400041245014900055210006900204260009700273300001200370490000800382520099300390653002101383653002601404653002201430653002801452653002801480100002701508700001301535700002601548856013001574       2009                        eng d  a0944-501300aPurification and characterization of putative alkaline [Ni-Fe] hydrogenase from unicellular marine green alga, tetraselmis kochinensis NCIM 16050 aPurification and characterization of putative alkaline NiFe hydr  aOFFICE JENA, P O BOX 100537, 07705 JENA, GERMANYbELSEVIER GMBH, URBAN & FISCHER VERLAGcFEB  a131-1370 v1643 a<p>Hydrogenase enzyme from the unicellular marine green alga Tetraselmis kochinensis NCIM 1605 was purified 467 fold to homogeneity. The molecular weight was estimated to be similar to 89kDa by SDS-PAGE. This enzyme consists of two subunits with molecular masses of similar to 70 and similar to 19 kDa. The hydrogenase was found to contain 10 g atoms of Fe and 1 g of atom of Ni per mote of protein. The specific activity of hydrogen evolution was 50 mu mol H-2/mg/h of enzyme using reduced methyl viologen as an electron donor. This hydrogenase enzyme has pl value similar to 9.6 representing its alkaline nature. The absorption spectrum of the hydrogenase enzyme showed an absorption peak at 425 nm indicating that the enzyme had iron-sulfur clusters. The total of 16 cysteine residues were found per mote of enzyme under the denaturing condition and 20 cysteine residues in reduced denatured enzyme indicating that it has two disulfide bridges. (C) 2007 Published by Elsevier GmbH.</p>10aCharacterization10aChemical modification10aNi-Fe hydrogenase10aTetraselmis kochinensis10aUnicellular green algae1 aBhosale, Siddharth, H.1 aPant, A.1 aKhan, Mohammad, Islam  uhttps://library.ncl.res.in/content/purification-and-characterization-putative-alkaline-ni-fe-hydrogenase-unicellular-marine-0