| pubmed-article:16928192 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16928192 | lifeskim:mentions | umls-concept:C0085089 | lld:lifeskim |
| pubmed-article:16928192 | lifeskim:mentions | umls-concept:C1721101 | lld:lifeskim |
| pubmed-article:16928192 | lifeskim:mentions | umls-concept:C0008260 | lld:lifeskim |
| pubmed-article:16928192 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:16928192 | lifeskim:mentions | umls-concept:C1148926 | lld:lifeskim |
| pubmed-article:16928192 | lifeskim:mentions | umls-concept:C0253830 | lld:lifeskim |
| pubmed-article:16928192 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:16928192 | pubmed:dateCreated | 2006-11-22 | lld:pubmed |
| pubmed-article:16928192 | pubmed:abstractText | Magnesium chelatase inserts Mg2+ into protoporphyrin IX and is the first unique enzyme of the chlorophyll biosynthetic pathway. It is a heterotrimeric enzyme, composed of I- (40 kDa), D- (70 kDa) and H- (140 kDa) subunits. The I- and D-proteins belong to the family of AAA+ (ATPases associated with various cellular activities), but only I-subunit hydrolyses ATP to ADP. The D-subunits provide a platform for the assembly of the I-subunits, which results in a two-tiered hexameric ring complex. However, the D-subunits are unstable in the chloroplast unless ATPase active I-subunits are present. The H-subunit binds protoporphyrin and is suggested to be the catalytic subunit. Previous studies have indicated that the H-subunit also has ATPase activity, which is in accordance with an earlier suggested two-stage mechanism of the reaction. In the present study, we demonstrate that gel filtration chromatography of affinity-purified Rhodobacter capsulatus H-subunit produced in Escherichia coli generates a high- and a low-molecular-mass fraction. Both fractions were dominated by the H-subunit, but the ATPase activity was only found in the high-molecular-mass fraction and magnesium chelatase activity was only associated with the low-molecular-mass fraction. We demonstrated that light converted monomeric low-molecular-mass H-subunit into high-molecular-mass aggregates. We conclude that ATP utilization by magnesium chelatase is solely connected to the I-subunit and suggest that a contaminating E. coli protein, which binds to aggregates of the H-subunit, caused the previously reported ATPase activity of the H-subunit. | lld:pubmed |
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| pubmed-article:16928192 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16928192 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16928192 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16928192 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16928192 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16928192 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16928192 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:16928192 | pubmed:author | pubmed-author:Al-KaradaghiS... | lld:pubmed |
| pubmed-article:16928192 | pubmed:author | pubmed-author:OlssonUlfU | lld:pubmed |
| pubmed-article:16928192 | pubmed:author | pubmed-author:HanssonMatsM | lld:pubmed |
| pubmed-article:16928192 | pubmed:author | pubmed-author:WillowsRobert... | lld:pubmed |
| pubmed-article:16928192 | pubmed:author | pubmed-author:SirijovskiNic... | lld:pubmed |
| pubmed-article:16928192 | pubmed:author | pubmed-author:LundqvistJoak... | lld:pubmed |
| pubmed-article:16928192 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16928192 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16928192 | pubmed:volume | 400 | lld:pubmed |
| pubmed-article:16928192 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16928192 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16928192 | pubmed:pagination | 477-84 | lld:pubmed |
| pubmed-article:16928192 | pubmed:dateRevised | 2010-9-16 | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:meshHeading | pubmed-meshheading:16928192... | lld:pubmed |
| pubmed-article:16928192 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16928192 | pubmed:articleTitle | ATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact. | lld:pubmed |
| pubmed-article:16928192 | pubmed:affiliation | Department of Biochemistry, Lund University, Box 124, SE-22100 Lund, Sweden. | lld:pubmed |
| pubmed-article:16928192 | pubmed:publicationType | Journal Article | lld:pubmed |
